Credit Hours - 3

Biochemical techniques encompass a wide range of methods for analyzing and manipulating biological molecules. These include:

• Acid-Base Chemistry
  • Titration techniques
  • pH measurement
  • Buffer preparation and function
  • Determination of pK values

• Biomolecule Analysis 

  a. Carbohydrates

  • Qualitative analysis
  • Glucose estimation (Folin-Wu method)
  • Glycogen isolation
  • Hydrolysis rate determination
  • Chromatography of hydrolysis products

  b. Proteins

  • Qualitative analysis
  • Quantitative methods: • Folin-Lowry method • Biuret method • Ultraviolet absorption
  • Amino acid determination (ninhydrin method)
  • Protein preparation, purification, and standardization (e.g., serum proteins, cytochrome C)

  c. Lipids

  • Qualitative analysis
  • Solubility tests
  • Emulsification properties
  • Iodine number determination
  • Acid value measurement
  • Serum lipid separation
• Separation Techniques
  • Chromatography: • Paper chromatography • Thin-layer chromatography (TLC) • Column chromatography
  • Electrophoresis: • Paper electrophoresis • Gel electrophoresis

Credit Hours - 3

Biomolecules form the foundation of life, ranging from simple monomers to complex supramolecules. Carbohydrates, including mono-, di-, oligo-, and polysaccharides, play crucial structural and storage roles, exhibiting phenomena like stereoisomerism and mutarotation. Lipids encompass a diverse group including fatty acids, triacylglycerols, phospholipids, sphingolipids, steroids, and eicosanoids, with some forming lipoproteins and glycolipids vital for cell recognition and signaling. Proteins, built from essential and non-essential amino acids, display complex hierarchical structures (primary to quaternary) and serve various functions, including as enzymes. Nucleic acids, composed of nucleotides, form the genetic blueprint as DNA and RNA, orchestrating replication, transcription, and translation. Other critical cellular molecules include porphyrins, vitamins, coenzymes, alkaloids, and inorganic ions, each playing unique roles in biological processes. This intricate interplay of biomolecules underpins the chemistry of life, from simple reactions to complex cellular functions.

Credit Hours - 2

Structure and Bonding provides a fundamental understanding of atomic and molecular architecture in chemistry. It begins with an exploration of atomic structure, using quantum mechanical principles to explain electron configurations and orbitals. The course then examines periodic trends, relating atomic structure to elemental properties. Students learn about various types of chemical bonds—ionic, covalent, and metallic—and use theories like VSEPR and hybridization to predict molecular shapes. Intermolecular forces, including hydrogen bonding and van der Waals interactions, are covered to explain physical properties of substances. The curriculum introduces basic concepts in solid-state chemistry and coordination compounds. Throughout the course, students apply their knowledge to interpret simple spectroscopic data and understand how bonding influences the reactivity and properties of molecules. This foundational course equips undergraduates with essential concepts for advanced chemistry studies and provides insight into the molecular basis of natural phenomena.

 CopyRetry

Credit Hours - 2

This course introduces students to the core area of physical chemistry, based around the themes of systems, states and processes. Topics covered are quantum mechanics and structure, chemical thermodynamics, phase changes, and chemical kinetics. Throughout the course, the relationship between physical phenomena and the molecular structure and reactions underpinning advanced materials will be highlighted. This content is designed to complement other 2000 level Chemistry courses which have a synthetic focus. The laboratory component provides training in a range of theoretical and applied physical chemistry techniques which are relevant to both industrial and research settings.A good understanding of physical chemistry is important to students intending to complete a major or minor study in chemistry, and will also be valuable for students studying engineering.

Credit Hours - 2

This undergraduate organic chemistry course delves into stereochemistry, alkene reactions, and the chemistry of alcohols and ethers. Students explore compounds with multiple chiral centers, including meso compounds and threo/erythro isomers. The course covers racemic mixtures and their resolution methods, as well as stereoisomerism in cyclic compounds, focusing on cyclohexane conformations. Alkene chemistry emphasizes ozonolysis, detailing its mechanism and applications in structure determination. For alcohols, the curriculum covers preparation methods such as hydration of alkenes, oxymercuration, hydroboration, and Grignard reactions. Alcohol reactions include oxidation (e.g., using PCC, Jones reagent), dehydration, and esterification. Ether chemistry encompasses Williamson synthesis, dehydration of alcohols, and reactions like HI cleavage and Claisen rearrangement for allyl ethers. Throughout, the course emphasizes reaction mechanisms, stereochemical considerations, and practical applications, providing students with a comprehensive understanding of these fundamental organic chemistry concepts.

Credit Hours - 2

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Credit Hours - 3

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Credit Hours - 2

This introductory course provides a comprehensive overview of the structure and functions of essential biomolecules, focusing on carbohydrates, lipids, proteins, and nucleic acids. Students will explore the classification, structural features, and functional properties of these key molecular components of life. The curriculum covers the diverse roles of carbohydrates in energy storage and cell recognition, the importance of lipids in membrane structure and signaling, the complex hierarchy of protein structure and its relation to function, and the critical role of nucleic acids in information storage and transfer. Additionally, the course introduces the structural organization of prokaryotic and eukaryotic cells, highlighting the differences between plant and animal cells. To complement the theoretical knowledge, students will gain familiarity with fundamental biochemical techniques used to study cellular components, including centrifugation, chromatography, electrophoresis, and basic spectroscopy. This foundation in biomolecular structure and cellular organization will equip students with the necessary background for advanced studies in biochemistry, molecular biology, and related life sciences.

Credit Hours - 3

This comprehensive course on biochemical metabolism covers the intricate pathways of carbohydrate, lipid, and amino acid processing in living organisms. In carbohydrate metabolism, students explore the digestion process, glycolysis, and the various fates of pyruvate across different organisms. The course delves into the tricarboxylic acid (TCA) cycle, pentose phosphate pathway, and the metabolism of non-glucose monosaccharides. It also covers anabolic processes like gluconeogenesis and glycogenesis, as well as unique pathways such as the Calvin-Benson cycle, Cori cycle, and glyoxylate cycle. Regulatory mechanisms and metabolic disorders related to carbohydrates are also discussed.

Lipid metabolism is examined in detail, starting with the digestion of triacylglycerols and the roles of various lipases. The course covers beta-oxidation of fatty acids, the fate of its products, and the synthesis of fatty acids, triacylglycerols, and cholesterol. Regulatory aspects of lipid metabolism are emphasized to understand the balance between catabolic and anabolic processes.

The section on amino acid metabolism begins with protein digestion and explores the fundamental processes of transamination, deamination, and decarboxylation. Students learn about the urea cycle, the fate of carbon skeletons, and the metabolism of specific amino acids, including aromatic and sulfur-containing variants. The synthesis of amino acids and inborn errors of metabolism are also covered, along with regulatory mechanisms.

The course concludes with a focus on bioenergetics, exploring the concepts of free energy in biochemical reactions, the role of ATP in metabolic processes, and various phosphorylation mechanisms (substrate-level, oxidative, and photo-phosphorylation). Students gain insights into energy coupling in metabolic reactions and the effects of uncoupling agents. This comprehensive approach provides a solid foundation in understanding the complex interplay of metabolic pathways and energy transformations in living systems.

Credit Hours - 2

This comprehensive course on Laboratory Management covers essential principles and practices for effective leadership in laboratory settings. It begins with organizational structures and leadership concepts, progressing through management functions and decision-making processes. The curriculum delves into Human Resource Management, addressing guidelines, job analysis, supervision, and professional development. Financial Management is explored, focusing on budgeting, cost/benefit analysis, and service justification. The Operations section covers laboratory design, equipment selection, workflow analysis, automation concepts, inventory control, and marketing strategies. Quality Assurance and Quality Control principles are emphasized, introducing students to quality management systems and international laboratory standards such as ISO 9001, ISO/IEC 17025, and ISO 15189, as well as Good Laboratory Practice (GLP). Throughout the course, ethical considerations in laboratory management are integrated, ensuring students understand the importance of maintaining professional integrity. This holistic approach equips future laboratory managers with the knowledge and skills needed to effectively oversee personnel, finances, operations, and quality in various laboratory environments, while adhering to ethical standards and regulatory requirements.

Credit Hours - 3

This advanced biochemistry course focuses on enzyme-catalyzed reactions and their practical applications, culminating in a hands-on mini-project. Students explore the kinetics of enzymatic reactions, examining how factors such as enzyme concentration, pH, temperature, substrate concentration, and the presence of activators or inhibitors affect reaction rates. The concept of enzyme specificity is thoroughly investigated. Practical exercises include studying protease activity in plant extracts and purifying enzymes from plant juice, providing real-world context to theoretical concepts. The course emphasizes the analytical applications of enzymes, such as the estimation of urea in urine. The highlight of the course is a mini-project where students isolate, purify, and characterize a known enzyme, offering a comprehensive, hands-on experience in enzyme biochemistry. This project integrates various techniques learned throughout the course, allowing students to apply their knowledge in a research-like setting. By combining theoretical understanding with practical skills, this course prepares students for advanced work in enzymology and biochemical research.

Credit Hours - 2

This comprehensive course equips you with the tools to understand, analyze, and interpret data effectively.

Course Structure:

• Data Fundamentals: Grasp the difference between discrete and ordinate data, and harness descriptive statistics like mean and standard deviation to unveil patterns.
• Statistical Principles: Explore the power of statistics in drawing conclusions from samples, delve into Gaussian and non-Gaussian distributions, and master concepts like confidence intervals, p-values, and statistical significance. Gain an alternative perspective with the Bayesian approach to interpreting data.
• Data Presentation: Master the art of communicating your findings with clear tables, informative histograms, scatter plots, bar charts, and box plots.
• Data Analysis Techniques: Uncover relationships and differences in data using methods like multiple comparisons, ANOVA (Analysis of Variance) for comparing groups, and survival data analysis. Explore techniques for analyzing categorical data with odds ratios and proportions tests. Learn to identify correlations and build prediction models with linear regression. Master the skill of choosing the right statistical test for your specific research question.
• Experimental Design: Design sound experiments by identifying response variables and influencing factors. Grasp the importance of replication and randomization in controlling for bias. Learn to minimize errors by understanding how timing, location, and other factors can impact your results.
• Statistical Software Applications: Put theory into practice with popular software packages like Excel and Minitab.

By the end of this course, you'll be able to:

• Understand and interpret different data types.
• Apply descriptive statistics to summarize data.
• Grasp core statistical principles like sampling, distributions, and hypothesis testing.
• Communicate findings effectively with clear data presentations.
• Choose and implement appropriate statistical analysis techniques for various research questions.
• Design robust experiments that minimize bias and error.
• Utilize popular statistical software packages for real-world data analysis.

Credit Hours - 3

This comprehensive course explores the intricate world of nucleic acid metabolism and genetic information flow. It begins with an in-depth study of purine and pyrimidine biosynthesis, including their regulatory mechanisms, and extends to the structure and properties of nucleosides and nucleotides. The biosynthesis of deoxyribonucleotides and thymidylate is covered, along with salvage pathways. The course then delves into DNA and chromosome structure, examining the evidence for DNA as the carrier of genetic information and exploring its primary, secondary (A, B, and Z forms), and tertiary structures. Students learn about the elucidation of DNA structure, including the Watson and Crick double helix model, and the structural differences between RNA and DNA. DNA sequencing methods and chromosomal organization, including nucleosome structure, are also addressed. The mechanism of DNA replication in both prokaryotes and eukaryotes is thoroughly explored, covering the evidence for semi-conservative replication, DNA replicating enzymes, and the directionality of replication. Finally, the course examines transcription mechanisms in prokaryotes and eukaryotes, the features of transcription units, characteristics of different RNA types, RNA modification and processing, and the phenomenon of reverse transcription. This comprehensive approach provides students with a solid foundation in molecular genetics and biochemistry.

Credit Hours - 3

This comprehensive course delves into the fascinating world of aromatic compounds, a class of organic molecules renowned for their unique stability and diverse applications.

• The Essence of Aromaticity: We begin by exploring the concept of aromaticity, delving into the electronic and structural characteristics that govern aromatic character. Explore the Hückel's rule and its implications for aromatic stability.
• Visualization Tools: Learn to utilize molecular orbital theory and resonance structures to visualize the delocalized electron cloud that is a hallmark of aromatic compounds.
• Non-benzenoid Aromatic Systems: Discover that aromaticity extends beyond benzene! Explore various heterocyclic and polycyclic aromatic compounds that exhibit aromatic character.
• Electrophilic Aromatic Substitution (EAS): Uncover the fundamental mechanism of EAS reactions, the workhorse for introducing new functional groups onto aromatic rings. Analyze the role of Lewis acids as catalysts and explore the factors that influence the regioselectivity (position of substitution) and reactivity of different aromatic substrates.
• Synthetic Applications of EAS: Witness the power of EAS reactions in organic synthesis. Learn how to prepare a diverse array of aromatic compounds with valuable functionalities like halides, nitro groups, alkyl groups, and more. Explore the applications of these compounds in pharmaceuticals, dyes, and polymers.
• Nucleophilic Aromatic Substitution (NAS): While less common than EAS, delve into the mechanisms of NAS reactions and the conditions required for successful substitution. Explore the reactivity of different nucleophiles with aromatic rings.
• Synthesis Strategies: Explore various methods for constructing polynuclear aromatic compounds, including coupling reactions, cyclization reactions, and condensation reactions.
• Reactivity of Polynuclear Aromatic Compounds: Learn how the presence of multiple aromatic rings influences the reactivity of these complex molecules. Explore their unique properties and potential applications in materials science and organic electronics.

Credit Hours - 2

This comprehensive course explores the fascinating world of viruses, the enigmatic infectious agents that blur the line between living and non-living entities. We'll examine their classification, structure, replication, and interaction with host cells, equipping you to understand these pervasive pathogens.

• Classification Systems: We begin by examining the various systems used to classify viruses, based on factors like genome type (DNA/RNA, single/double stranded), structure (enveloped/non-enveloped), and replication strategy (lytic/lysogenic). Explore the International Committee on Taxonomy of Viruses (ICTV) and its role in standardizing viral classification.
• Particle Structure and Stability: Unravel the intricate architecture of viral particles, including capsids (protein shells), envelopes (lipid bilayers), and nucleocapsids (complexes of viral nucleic acid and proteins). Learn about factors that influence viral stability in the environment and within host organisms, such as capsid composition, pH, and temperature.
• Genome Diversity: Discover the remarkable diversity of viral genomes, encompassing single-stranded (ss) and double-stranded (ds) DNA or RNA molecules. Explore the unique features of each type and their implications for replication and evolution (e.g., ssRNA viruses with high mutation rates).
• Viral Replication: Demystify the fascinating process of viral replication, from attachment and entry into host cells to viral gene expression, protein synthesis, assembly of new viral particles, and their release. Explore the differences in replication strategies between various virus types, such as the lytic cycle (immediate cell lysis) and the lysogenic cycle (viral genome integration into host DNA).
• Cell-to-Cell Movement: Learn about the mechanisms viruses employ to move from one infected cell to another, ensuring their continued propagation. Explore different modes of cell-to-cell movement like budding (protrusion and pinching off) and cell-to-cell fusion (creation of multinucleated cells).
• Viral Transmission: Uncover the diverse routes by which viruses are transmitted between hosts, including direct contact, airborne droplets, bodily fluids (blood, saliva), and vectors like insects (mosquitoes) and animals (ticks).
• Viral Genetics: Explore the unique features of viral genomes and their susceptibility to mutation. Learn how mutations can contribute to viral evolution, emergence of new strains, and potential drug resistance.
• Virus-Host Interactions: Delve into the intricate dance between viruses and their hosts. Explore how viruses manipulate host cell machinery for their own replication (e.g., hijacking ribosomes for protein synthesis) and how host immune systems attempt to defend against viral invasion (e.g., antibody production and immune cell activation).
• Electron Microscopy: Discover the power of electron microscopy in visualizing the morphology and structure of viral particles at high magnification.
• Serology and Immunochemistry: Learn how serological techniques like enzyme-linked immunosorbent assay (ELISA) can be used to diagnose viral infections by detecting antibodies produced in response to the virus.
• Molecular Methods: Explore the power of molecular methods like hybridization (identifying specific viral sequences), PCR (amplifying viral DNA), and RT-PCR (reverse transcription PCR for RNA viruses) for detecting and characterizing viral nucleic acids.
• Viral Epidemiology: Unravel the patterns of viral outbreaks and how factors like population density, human behavior, and vaccination coverage influence their spread. Explore strategies for disease surveillance (tracking outbreaks) and outbreak control (containment measures).
• Plant, Animal, and Bacterial Viruses: Focus on specific examples of viruses that impact different kingdoms of life, including the cocoa swollen shoot virus (plant), HIV and bird flu virus (animals), and bacteriophages (bacteria). Explore their unique characteristics, disease processes, and potential control measures (e.g., plant breeding for resistance, antiviral drugs, vaccines).

Credit Hours - 2

This comprehensive industrial microbiology course explores how microorganisms revolutionize industries like food production and environmental cleanup. We'll examine the importance of these tiny powerhouses and the specific microbes used in various applications. Techniques for optimizing large-scale fermentation processes, including media formulation and strain improvement, will be covered. The course then delves into preventing microbial contamination through regulatory measures and quality control. We'll explore the unique biology of molds, yeasts, and bacteria used in industry, alongside techniques for culturing and manipulating them for large-scale product generation. Finally, the course surveys the diverse applications of industrial microbiology, from producing pharmaceuticals and food to bioremediation, equipping you with a deep understanding of this transformative field.

Credit Hours - 3

The course on Molecular Biology Tools and Techniques encompasses a comprehensive exploration of essential methodologies and applications. Key topics include agarose and polyacrylamide gel electrophoresis for DNA and protein separation; Northern and Southern blots for RNA and DNA hybridization analysis, respectively; and Western blots for protein detection. The course delves into the principles of PCR, RAPD, and RFLP for nucleic acid amplification and polymorphism analysis. It covers the purification and characterization of nucleic acids, including extraction techniques, concentration and molecular weight determination, and differentiation of RNA/DNA and single/double-stranded nucleic acids. Modifying enzymes such as restriction endonucleases, DNAse, RNAse, ligases, and polymerases are thoroughly examined. Recombinant DNA technology is a focal point, discussing cloning and expression vectors, creation of recombinant molecules, and transformation systems in both prokaryotic and eukaryotic hosts. Techniques for colony screening, plasmid isolation, and characterization, as well as transduction and conjugation, are included. The course also covers nucleotide sequencing via Maxam-Gilbert chemical cleavage and Sanger’s enzymatic synthesis, along with deletion and insertion mutagenesis. Gene expression detection methods, including RT-PCR, real-time RT-PCR, and microarrays, are explained. The practical applications of these techniques in medicine, agriculture, and industry are highlighted, showcasing their relevance and impact in various fields

Credit Hours - 2

The course on Cellular Regulation and Signaling explores various types of cellular regulation, including endocrine, paracrine, autocrine, and direct cell-to-cell communication. Primary signaling molecules such as growth factors, hormones, and neurotransmitters are examined. The structure and properties of receptors are discussed, covering cell surface and intracellular receptors, G-protein coupled receptors, and receptor tyrosine kinases. Key concepts such as conserved domains, ligand recognition, binding characteristics, receptor dimerization, phosphorylation, docking sites, and substrate interactions are thoroughly explained.

The course investigates guanine nucleotide binding-protein switches, focusing on both heterotrimeric and monomeric forms, and delves into G-protein regulators like GTPase-activating proteins and guanine nucleotide exchange factors, exemplified by Son of Sevenless and neurofibromin. The generation of second messengers, including cyclic AMP, cyclic GMP, inositol trisphosphate, diacylglycerol, and Ca2+, is explored.

Major signaling cascades are highlighted, including the Ras-mitogen-activated protein kinase pathway, phosphatidylinositol-3-kinase and Akt pathway, Janus kinase and Signal Transducer and Activator of Transcription pathway (JAK-STAT), and nitric oxide-guanylyl cyclase signaling. The course covers the roles of effectors and transcription factors, mechanisms of signal amplification, signal diversity, cross-talk between pathways, and signal termination.

Credit Hours - 2

The course on Tropical Parasitic Diseases delves into . The course examines the intricate biochemistry  and the pathophysiology of major tropical parasitic diseases, including malaria, trypanosomiasis, filariasis, schistosomiasis, and gastrointestinal worm infestations, emphasizing the complex host-parasite interrelationships. Key topics include the molecular basis of the parasites' life cycles, their survival strategies within the host, and the host's immune response.

The course highlights the molecular mechanisms underlying the pathogenesis of these diseases. For malaria, the focus is on Plasmodium species' lifecycle and its interaction with red blood cells. In trypanosomiasis, the emphasis is on the antigenic variation of Trypanosoma species and their evasion of the host immune system. Filariasis is explored through the lens of filarial worms' lifecycle and their impact on the lymphatic system. Schistosomiasis discussions center on Schistosoma species and their unique life cycle involving snail intermediate hosts and human definitive hosts. Gastrointestinal worm infestations cover a range of helminths and their mechanisms for nutrient absorption and immune evasion.

A significant portion of the course is dedicated to the molecular basis of chemotherapeutic attacks on parasites, exploring how drugs target specific biochemical pathways of the parasites. The course examines various classes of antiparasitic drugs, their mechanisms of action, and the challenges of drug resistance. This comprehensive study equips students with a deep understanding of tropical parasitic diseases, their biochemical underpinnings, and current strategies for treatment and control.

Credit Hours - 1

The course on Scientific Writing and Communication encompasses a detailed review of language structure and usage, essential for effective scientific communication. It explores the different types of scientific reports, including seminars, research papers, proposals, and posters, providing a comprehensive understanding of their unique formats and purposes.

The structure of scientific reports is thoroughly examined, covering all critical components: the title, authors, abstract/summary, table of contents, and glossary. The course delves into the essential sections of a scientific report, such as the introduction (context, focus, justification), materials and methods, results, discussion, conclusion, references, and appendices.

Emphasis is placed on writing style and rules, highlighting important dos and don'ts to maintain clarity and precision in scientific writing. The course addresses the critical issue of plagiarism, teaching students how to avoid it and maintain academic integrity.

Additionally, students are required to attend all departmental seminars, presented by either internal or external speakers. They must actively participate in journal clubs by presenting journal articles, and they are also expected to present their research proposals and project seminars. This hands-on approach ensures that students gain practical experience in scientific communication and presentation, preparing them for professional scientific discourse.

Credit Hours - 3

The course on Immunology covers the essential aspects of the immune system and its role in health and disease. Key topics include:

1. Defense Systems: Understanding the concepts of self and non-self, and distinguishing between innate and acquired immunity. The course covers the cells and organs involved in these immune responses, as well as the mechanisms of humoral and cell-mediated immunity.
2. Antigens: Delving into the concepts of immunogenicity and antigenicity, the course explores the chemical nature of antigens, including bacterial, viral, and synthetic antigens.
3. Antibodies: Focusing on the structure and function of immunoglobulins, the course discusses various theories of antibody production. It also covers the methods for producing polyclonal and monoclonal antibodies, with an emphasis on hybridoma technology.
4. Antigen-Antibody Interactions: The course explains the mechanisms of agglutination and precipitation, as well as various immunoassays used to detect these interactions.
5. The Complement System: Students learn about the components and activation of the complement system via classical and alternative pathways, and how these processes are regulated.
6. Vaccines: Current methods for vaccine development are explored, along with immune regulation and tolerance. The course also covers immunopathology, including hypersensitivity, immunodeficiency, and autoimmunity, as well as transplantation immunology and the mechanisms involved in tissue rejection.
7. Cytokines: General properties and biological activities of selected cytokines are examined, highlighting their role in immune responses.
8. Immunology of Diseases of Public Health Interest: The course addresses the immunological aspects of significant diseases such as HIV/AIDS, malaria, and schistosomiasis, focusing on their impact on public health and the immune system's response to these diseases.

This comprehensive curriculum equips students with a thorough understanding of immunology, preparing them to address complex immunological challenges in health and disease contexts.

Credit Hours - 2

This course provides hands-on experience with advanced molecular biotechnology techniques, focusing on their applications in biochemistry and related fields. Students will gain practical skills in various methods used to manipulate and analyze nucleic acids and proteins, alongside proficiency in bioinformatics tools for in silico design and analysis.

Key Topics and Techniques:

1. Agarose and Polyacrylamide Gel Electrophoresis:
   • Agarose Gel Electrophoresis: Techniques for separating and analyzing DNA fragments.
   • Polyacrylamide Gel Electrophoresis (PAGE): Methods for separating and analyzing proteins and small DNA fragments.
2. Blotting and Hybridization Techniques:
   • Southern Blotting: Procedures for detecting specific DNA sequences.
   • Northern Blotting: Techniques for detecting specific RNA sequences.
   • Western Blotting: Methods for detecting and analyzing specific proteins.
3. PCR and Related Techniques:
   • Polymerase Chain Reaction (PCR): Protocols for amplifying DNA sequences.
   • Random Amplified Polymorphic DNA (RAPD): Methods for analyzing genetic diversity.
   • Restriction Fragment Length Polymorphism (RFLP): Techniques for genetic mapping and polymorphism analysis.
4. Nucleic Acid Purification and Characterization:
   • Extraction and Purification: Techniques for isolating DNA and RNA from various sources.
   • Concentration and Molecular Weight Determination: Methods for quantifying and estimating the size of nucleic acids.
   • Species Differentiation: Techniques for differentiating RNA/DNA and single/double-stranded nucleic acids.
5. Bioinformatics and In Silico Design:
   • Identification of Fungi: Using bioinformatics tools for fungal identification and classification.
   • Cloning Design: Utilizing in silico design tools such as SoftBerry, SMART, Clustal Omega, NEB Cutter, and NEB Cloner for designing cloning experiments.
   • Sequence Analysis: Application of bioinformatics tools for sequence alignment, gene prediction, and analysis.

Course Requirements:

• Attendance: Mandatory participation in all lab sessions.
• Lab Reports: Detailed documentation of experimental procedures, results, and analyses.

Credit Hours - 2

This course provides an in-depth introduction to practical clinical biochemistry, emphasizing laboratory investigations and specimen collection. Students will learn about the principles and application of analytical methods and standardization techniques, including calibration standards, precision, accuracy, sensitivity, and specificity. The curriculum covers a comprehensive review of analytical and separation methods used in clinical biochemistry for detecting and quantifying metabolites, ions, and enzymes. Essential skills such as report writing and result interpretation will be developed, with a focus on understanding reference values and the factors influencing them.

The course also delves into organ function disorders and their diagnostic tests, including those for the gastrointestinal system, liver, kidneys, heart, pituitary gland, pancreas, thyroid, adrenal glands, and gonads. Additionally, students will study the composition and abnormalities of body fluids, including water and electrolyte balance, acid-base disorders, and oxygen transport.

An exploration of disorders of metabolism, particularly inborn errors of metabolism, will cover lipids, carbohydrates, amino acids, proteins, purines, and porphyrins. 

Credit Hours - 2

This course provides a comprehensive exploration of xenobiotic metabolism, focusing on the pathways, enzymology, and pharmacological and toxicological aspects related to foreign compounds in biological systems. Students will delve into the intricate processes of Phase I and II reactions involved in xenobiotic metabolism.

Key Topics Covered:

1. Pathways of Xenobiotic Metabolism:
   • Detailed examination of Phase I and Phase II reactions involved in the biotransformation of xenobiotics within biological systems.
2. Enzymology and Molecular Mechanisms:
   • Cytochrome P-450-Dependent Mixed-Function Oxidation Reactions: Mechanisms and roles of cytochrome P-450 enzymes in metabolizing xenobiotics.
   • Microsomal Flavin-Containing Monooxygenases: Function and contribution to xenobiotic metabolism.
   • Prostaglandin Synthetase, Reduction Enzymes, Epoxide Hydrolase, and Conjugating Enzymes: Roles of these enzymes in detoxification and activation pathways of xenobiotics.
3. Factors Affecting Xenobiotic Metabolism:
   • Internal Factors: Genetic variability, enzyme induction/inhibition, and age-related changes.
   • External Factors: Environmental exposures, diet, and interactions with other drugs or chemicals.
4. Pharmacological Aspects:
   • Activation and Deactivation: Mechanisms altering the pharmacological response of xenobiotics.
   • Drug Uptake and Distribution: Processes influencing the absorption, distribution, metabolism, and excretion (ADME) of xenobiotics.
   • Enterohepatic Circulation: Impact on xenobiotic metabolism and elimination.
5. Toxicological Aspects:
   • Metabolic Activation: Consequences leading to increased toxicity, including carcinogenesis, mutagenesis, teratogenesis, and specific organ toxicities (e.g., pulmonary, hepatic, renal).
   • Deactivation: Mechanisms leading to decreased toxicity and detoxification pathways.
   • Balance Between Toxification and Detoxifying Pathways: Understanding the equilibrium between activating and deactivating processes in xenobiotic metabolism.

This course integrates pharmacological and toxicological perspectives on xenobiotic metabolism, equipping students with essential knowledge to assess the risks and benefits associated with drug metabolism and environmental exposures.

Credit Hours - 2

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Credit Hours - 2

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Credit Hours - 2

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Credit Hours - 3

This course covers essential biochemical analysis techniques used in laboratories, including acid-base reactions, buffer preparation, chromatography, and both qualitative and quantitative analysis of biomolecules such as carbohydrates, proteins, and lipids. Titration and pH measurement are crucial for determining acid and base concentrations, while buffer preparation ensures pH stability in reactions. Qualitative analysis identifies carbohydrates through tests like Benedict's and proteins via the Biuret test, while lipids are analyzed for solubility, emulsification, and specific reactions such as the iodine number test. Quantitative protein analysis methods include the Folin-Lowry, Biuret, and UV absorption methods, with amino acids determined by the ninhydrin method. Protein purification involves techniques for serum proteins and cytochrome C. Separation methods like electrophoresis and chromatography (paper, TLC, column) are used for detailed biomolecular analysis. Quantitative carbohydrate analysis includes glucose estimation by the Folin-Wu method, glycogen isolation, hydrolysis rate determination, and chromatography of hydrolysis products. Lipids are quantitatively analyzed for solubility, emulsification, iodine number, acid value, and serum lipid separation. These techniques are fundamental for biochemical research and practical laboratory applications.

Credit Hours - 2

This course provides a comprehensive introduction to cell biology, focusing on the structure, function, and dynamics of cellular compartments in both prokaryotes and eukaryotes. Topics covered include:

• Cellular Compartments of Prokaryotes and Eukaryotes: Exploration of the organization, dynamics, and functions of cellular compartments in prokaryotic and eukaryotic cells. This includes an in-depth look at cellular membrane systems, their structure, and mechanisms of transport.
• Nucleus: Study of the nuclear envelope and matrix, emphasizing their roles in cell function and organization.
• Mitochondria and Chloroplasts: Detailed examination of these organelles, focusing on their biogenesis, evolution, and critical roles in cellular energy metabolism.
• Cell Division, Differentiation, and Development: Analysis of various aspects of cell division and development, including:
  • Bacterial division mechanisms.
  • Meiosis and gametogenesis in eukaryotes.
  • The eukaryotic cell cycle, covering mitosis and cytokinesis.
  • Processes of fertilization and early embryonic development, with an emphasis on positional information, homeotic genes, tissue-specific expression, nuclear and cytoplasmic interactions, growth factors, induction, environmental influences, and cellular polarity.
  • Differentiation of specialized cells in plant and animal tissues.

Credit Hours - 2

This course provides an in-depth study of enzymes, their properties, kinetics, and applications, covering the following key areas:

• Introduction to Enzymes: Understanding the fundamentals of enzyme catalysis compared to chemical catalysis, including concepts of activation energy, transition state, free energy change, and chemical equilibria. Exploration of the active site, substrate specificity, enzyme classification, enzyme assays, and linked or coupled enzyme reactions.
• Factors Affecting Enzyme Activity: Investigation of factors influencing enzyme activity such as reaction rate (v), substrate concentration ([S]), enzyme concentration ([E]), temperature (T), and pH. The role of coenzymes and prosthetic groups in enzymatic reactions.
• Enzyme Kinetics and Inhibition: Study of enzyme kinetics through the Michaelis-Menten model and graphical data representation using Lineweaver-Burk and Hanes plots. Examination of enzyme inhibition, including reversible inhibition (competitive, noncompetitive, and uncompetitive) and irreversible inhibition.
• Control of Enzyme Activity: Analysis of mechanisms regulating enzyme activity, including feedback regulation, allosteric enzymes, isozymes, covalent modification, and activation. Discussion of the regulation of enzyme synthesis and breakdown with examples such as the lac operon and tryptophan biosynthesis.
• Enzyme Purification: Techniques for cell disruption and a general strategy for enzyme purification. Emphasis on enzyme assays and units of enzyme activity.
• Application of Enzymes: Exploration of the practical applications of enzymes in health, agriculture, and industry, highlighting their importance and diverse utility.

Credit Hours - 3

This course provides a comprehensive overview of the key biochemical techniques used in modern research laboratories, focusing on chromatography, centrifugation, and electrophoresis.

Chromatography:

• Partition Coefficient and Chromatographic Systems: Introduction to the basis of separation techniques, including adsorption and partition based on polarity, ion-exchange based on ionic nature, and exclusion/gel based on molecular size and shape.
• Principles and Applications: Detailed study of various chromatographic methods such as High-Performance Liquid Chromatography (HPLC), Fast Protein Liquid Chromatography (FPLC), Gas-Liquid Chromatography (GLC), Thin Layer Chromatography (TLC), paper chromatography, chromatofocusing, and two-dimensional electrophoresis.
• Analytical Aspects: Examination of key parameters including retention time and volume, capacity ratio, peak resolution, theoretical plates/plate height, peak capacity, and techniques for internal and external standardization and analyte quantitation.

Centrifugation:

• Basic Principles: Understanding sedimentation, Relative Centrifugal Force (RCF), and the relationship between velocity (v), sedimentation coefficient (s), and gravitational force (G).
• Centrifuges and Rotors: Overview of different types of centrifuges and rotors, and their specific uses.
• Preparative Centrifugation: Techniques such as differential and density gradient centrifugation, including the preparation of gradients and recovery and monitoring of fractionates.
• Analytical Centrifugation: Methods for determining relative molar mass using sedimentation velocity and equilibrium methods, and assessing the purity and shape of macromolecules.

Electrophoresis:

• General Principles: Basics of electrophoretic separation.
• Low Voltage Thin Sheets: Techniques using paper, cellulose acetate, and thin layer electrophoresis.
• High Voltage Gels: Applications involving agarose and polyacrylamide gels, including native, gradient, and SDS-PAGE.
• Applications: Focus on determining the purity and molecular weight of biomolecules.

Credit Hours - 2

This course delves into advanced topics in organic chemistry, focusing on the structure, preparation, and reactivity of aldehydes, ketones, carboxylic acids, their derivatives, and amines. Key areas of study include:

Aldehydes and Ketones:

• Nucleophilic Addition Reactions: Examination of the mechanisms and outcomes of nucleophilic addition to carbonyl groups in aldehydes and ketones.
• Carbanions: Understanding the formation, stability, and reactions of carbanions, with emphasis on their role in organic synthesis.

Carboxylic Acids:

• Preparations and Reactions: Detailed study of various methods for preparing carboxylic acids and their typical reactions, including nucleophilic acyl substitution and decarboxylation.

Carboxylic Acid Derivatives:

• Preparations: Overview of the synthesis of carboxylic acid derivatives such as esters, amides, anhydrides, and acid chlorides.
• Reactions: Exploration of the reactivity and transformations of carboxylic acid derivatives, focusing on nucleophilic substitution and related mechanisms.

Amines:

• Preparations and Reactions: Comprehensive coverage of the synthesis of primary, secondary, and tertiary amines, along with their reactions, including alkylation, acylation, and the formation of diazonium salts.

Credit Hours - 2

This course provides a detailed exploration of the chemistry of s-block elements, specifically focusing on Groups IA, IIA, and IIB. Key topics include:

Systematic Chemistry of s-block Elements:

• Group IA (Alkali Metals): Examination of the properties, reactivity, and applications of alkali metals (Li, Na, K, Rb, Cs, Fr). Discussion of their occurrence, extraction, and typical compounds.
• Group IIA (Alkaline Earth Metals): Study of the characteristics, chemical behavior, and uses of alkaline earth metals (Be, Mg, Ca, Sr, Ba, Ra). Coverage of their natural sources, methods of isolation, and common compounds.
• Group IIB (Zinc, Copper, Mercury): Detailed analysis of the elements in Group IIB, including:
  • Zinc: Properties, industrial significance, biological roles, and key compounds.
  • Copper: Physical and chemical properties, major uses, and important complexes.
  • Mercury: Unique characteristics, toxicity, industrial applications, and notable compounds.

Organometallic Compounds:

• Organometallic Chemistry: Introduction to the synthesis, structure, bonding, and reactivity of organometallic compounds of s-block elements.
• Applications: Exploration of the roles of s-block organometallic compounds in various fields, including catalysis, material science, and pharmaceuticals.

Credit Hours - 3

This introductory course will focus on the structure and functions of biomolecules.  Topics to be covered include classification, structure and functional properties of the major biomolecules (carbohydrates, lipids, proteins and nucleic acids). Students will also be equipped with basic knowledge of the structural organization of prokaryotic and eukaryotic cells as well as biochemical techniques for studying cellular components.

Credit Hours - 2

This course continues the exploration of cell biology, with a focus on cellular communication, structural dynamics, protein synthesis, and the study of cells as organisms. Key topics include:

Cell Surface and Communication:

• Extracellular Matrix (ECM): Structure and function of the ECM, including cell walls in plants and fungi.
• Cell Adhesion and Junctions: Mechanisms of cell-cell adhesion, types of junctions (tight junctions, gap junctions, and desmosomes), and their roles in tissue integrity and communication.
• Signal Transduction: Pathways and mechanisms of signal transduction, including the roles of various receptors and second messengers.
• Receptor Function: Types and functions of cell surface receptors, including G-protein-coupled receptors, tyrosine kinase receptors, and ion channel receptors.
• Excitable Membrane Systems: Understanding of excitable membranes, focusing on nerve and muscle cells and the propagation of electrical signals.

Cytoskeleton, Motility, and Shape:

• Actin-based Systems: The role of actin in cell shape and movement, including detailed mechanisms of muscle contraction.
• Microtubule-based Systems: Functions of microtubules in cell division, intracellular transport, and maintenance of cell structure.
• Intermediate Filaments: Structure, function, and significance of intermediate filaments in maintaining cell integrity.
• Prokaryotic Systems: Overview of cytoskeletal elements in prokaryotes and their roles in cell shape and division.

Protein Synthesis and Processing:

• Regulation of Translation: Mechanisms controlling the translation of mRNA into proteins.
• Post-translational Modification: Various modifications proteins undergo after translation, including phosphorylation, glycosylation, and ubiquitination.
• Intracellular Trafficking: Pathways and mechanisms involved in the intracellular movement of proteins and organelles.
• Secretion and Endocytosis: Processes of protein secretion and the mechanisms of endocytosis and intracellular digestion.

Cells as Organisms:

• Bacterial Life Cycles: Study of the life cycles of bacteria, including reproduction and sporulation.
• Protozoa and Algae: Overview of the biology and life cycles of protozoa and algae, emphasizing their ecological roles and significance.
• Parasitic Protozoa and Fungi: Examination of parasitic protozoa and fungi, focusing on their life cycles, host interactions, and impacts as both free-living and parasitic organisms.

Credit Hours - 2

This hands-on course provides practical experience in enzyme-catalyzed reactions, enzyme kinetics, and the use of enzymes in analytical applications, along with a mini project focused on enzyme isolation and characterization. Key components include:

Enzyme-Catalyzed Reactions:

• Time Course of Reaction: Monitoring the progress of enzyme-catalyzed reactions over time to understand reaction kinetics.
• Effects of Various Factors on Reaction Rate:
  • Enzyme Concentration: Investigating how varying enzyme concentrations affect the reaction rate.
  • pH: Examining the influence of pH on enzyme activity and stability.
  • Temperature: Studying the effect of temperature on enzyme kinetics and the determination of optimal temperature.
  • Substrate Concentration: Analyzing how changes in substrate concentration impact the reaction rate and enzyme saturation.
  • Activators and Inhibitors: Exploring the effects of activators and inhibitors on enzyme activity and understanding different types of enzyme inhibition.
• Enzyme Specificity: Assessing the specificity of enzymes for their substrates.
• Protease Activity in Plant Extracts: Measuring and characterizing protease activity in various plant extracts.
• Purification of Enzymes from Plant Juice: Techniques for isolating and purifying enzymes from plant sources.
• Use of Enzymes as Analytical Tools: Practical applications of enzymes in analytical biochemistry, such as the estimation of urea in urine using urease.

Mini Project:

• Isolation, Purification, and Characterization of a Known Enzyme: A comprehensive project where students isolate a specific enzyme, purify it, and characterize its properties, including activity, kinetics, and substrate specificity.

Credit Hours - 2

This course provides a thorough understanding of the mechanisms governing metabolic pathways and their regulation, focusing on both fine and coarse control mechanisms, and the integration of metabolism across different tissues and physiological states. Key topics include:

Metabolic Control:

• Design of Metabolic Pathways: Principles underlying the design and organization of metabolic pathways.
• Regulatory Enzymes:
  • Fine Control: Mechanisms of enzyme regulation, including allosteric regulation, substrate/product feedback, feed-forward controls, and covalent modification.
  • Coarse Control: Regulation of enzyme synthesis through induction and repression.

Regulation of Fuel Metabolism:

• Pathways: Detailed study of the regulation of key metabolic pathways, including glycolysis, gluconeogenesis, glyceroneogenesis, glycogenolysis, glycogenesis, the Krebs cycle, lipogenesis, lipolysis, β-oxidation, ketogenesis, and amino acid metabolism.
• Role of Hormones: Examination of how hormones such as insulin, glucagon, and epinephrine regulate metabolism.
• DNA Binding Proteins: Understanding the roles of cyclic AMP response element-binding protein (CREB), carbohydrate response element-binding protein (ChREBP), and sterol regulatory element-binding protein (SREBP) in metabolic regulation.

Integration of Metabolism:

• Glucose Homeostasis and Transport: Mechanisms maintaining glucose homeostasis and the role of glucose transporters.
• Interrelationships Between Metabolic Pathways: Exploration of the interconnections between carbohydrate, lipid, and protein metabolism.
• Enzyme Profiles: Study of tissue- and organ-specific enzyme profiles.
• Interorgan Relationships: Examination of metabolic interactions among liver, brain, muscle, and adipose tissue under various physiological states such as fed, fasted, athletic activity, and pregnancy.

Credit Hours - 3

This course offers an in-depth exploration of the principles of bioenergetics, thermodynamics, and membrane biology, with a focus on the energetic processes within cells and the structure and function of biological membranes.

Overview of Chemical Thermodynamics:

• Key Concepts: Internal energy, enthalpy, entropy, Gibbs free energy, and the laws of thermodynamics.
• Processes: Distinction between spontaneous and non-spontaneous processes.
• Biochemical Applications: Free energy changes in biochemical reactions.

Principles of Thermodynamics in Cellular Energetics:

• Redox Systems: Understanding electron donors and acceptors, redox couples, redox potentials, electromotive force, and proton motive forces.

High Energy Compounds:

• Types: Phosphoric acid anhydrides, phosphoric-carboxylic acid anhydrides, phosphoguanidines, enolphosphates, and thiol esters.
• Energy Basis: Explanation of the high standard free energy of hydrolysis.
• ATP's Role: Central role of ATP in energy transfer, including phosphate group transfer potentials and substrate-level phosphorylation.
• Coupled Reactions: Energetics of coupled biochemical reactions.

ATP Synthesis and Utilization:

• Mitochondria and Chloroplasts: Review of structures and sources of energy.
• Electron Transport: Redox complexes involved in electron transport and proton gradient establishment.
• ATP Synthesis Mechanism: Coupling ATP synthesis to proton gradient dissipation, role of H+-ATPase, and thermogenesis.
• Cellular Work: ATP utilization in active membrane transport and mechanical work such as muscle contraction.

Membrane Structure and Function:

• Membrane Types and Functions: Chemical composition of membranes, including lipids, proteins, and carbohydrates.
• Lipid Properties: Amphipathic nature of lipids and their formation into monolayers, bilayers, liposomes, and micelles.
• Phospholipase Reactions: Reactions and roles of phospholipases in membrane dynamics.

Membrane Models and Properties:

• Historical Models: Dawson-Danielli and Singer-Nicholson models.
• Protein Types: Integral (e.g., glycophorin A, anion channel band 3, bacteriorhodopsin), lipid-anchored, and peripheral proteins.
• Membrane Components: Plasma membrane glycocalyx and its antigenic properties (e.g., RBC M and N, blood group O, A, and B).
• Membrane Dynamics: Evidence for the asymmetric, dynamic, and fluid-like nature of biomembranes, and roles in cell-cell recognition and fusion (e.g., flu virus and HIV infections).
• Membrane Biogenesis: Synthesis and transport of membrane lipids.

Membrane Preparation and Study:

• Study Methods: Physical, chemical, and biochemical methods for studying lipid bilayers and vesicles in eukaryotic and prokaryotic cells.

Membrane Transport:

• Thermodynamics: Principles governing membrane transport.
• Transport Modes and Types: Uniport, symport, antiport systems; simple diffusion, passive-mediated, active transport; Na/K pump, co-transport (e.g., Na/glucose pump in kidneys/intestines, galactose permease in E. coli), exocytosis, and endocytosis.
• Channels and Pores: Ligand-gated and voltage-gated channels, ionophores (valinomycin, gramicidin A, and nigericin).

Credit Hours - 3

This course provides an in-depth study of protein structure and function, focusing on the primary, secondary, tertiary, and quaternary levels, as well as protein-ligand interactions, allostery, and enzyme catalysis. Key topics include:

Primary Structure:

• Amino Acid Composition: Understanding the building blocks of proteins and their significance.
• Sequence Determination: Methods for determining the amino acid sequence of proteins.
• Synthesis of Peptides: Techniques for synthesizing peptides and the importance of primary structure.
• Covalent Modification: Various covalent modifications of polypeptides and their functional implications.

Secondary Structure:

• Peptide Bond: Structural implications of the peptide bond.
• Random Polymers: Characteristics of random polypeptide chains.
• Ramachandran Plot: Understanding permissible angles in polypeptide chains.
• Regular Conformations: Detailed study of α-helix, β-pleated sheets, and other helices (e.g., 3₁₀-helix).
• Super-Secondary Structures: Structures such as the coiled-coil α-helix.
• Fibrous Proteins Examples: Examination of α-keratins, silk fibroin, and collagen.

Tertiary Structure:

• Protein Folding: Evidence for and mechanisms of protein folding and unfolding.
• Structural Determination: Techniques such as X-ray crystallography to determine protein structures.
• Reverse Turns: Understanding β-turns and their role in protein folding.
• Super-Secondary Structures: Study of motifs, domains, and the differentiation between protein interiors and exteriors.
• Example: Detailed analysis of myoglobin.

Quaternary Structure:

• Aggregation: Mechanisms of protein aggregation into quaternary structures.
• Example: Detailed study of haemoglobin.

Protein-Ligand Interactions:

• Binding Sites: Examination of binding sites in haemoglobin and myoglobin.
• Oxygen and Carbon Monoxide Binding: Mechanisms of oxygen and carbon monoxide binding, and the micro-environment of haem iron.
• Hill Plot: Analysis of cooperative binding.
• Protein Engineering: Techniques and applications in modifying protein functions.

Allostery:

• Binding Site Interactions: Interaction between binding sites.
• Theoretical Models:
  • MWC Model: Mond-Wyman-Changeux concerted mechanism.
  • KNF Model: Koshland-Nemethy-Filmer sequential model.
• Allosteric Properties of Haemoglobin: Mechanisms of cooperative binding of oxygen, the Bohr effect, and binding of 2,3-bisphosphoglycerate (BPG).

Mechanism of Enzyme Catalysis:

• Catalysis Types: General acid-base catalysis and covalent catalysis.
• Coenzyme Catalysis: Role of coenzymes such as pyridoxal phosphate, thiamine pyrophosphate, ATP, coenzyme A, NAD(P)+, FAD/FMN.
• Enzyme Structure and Mechanism: Detailed study of selected enzymes.
  • Examples: Dehydrogenases, proteases, ribonuclease, lysozyme, glycolytic enzymes like phosphofructokinase (PFK).

Physical Forces:

• Maintaining Structure: Analysis of the physical forces (e.g., hydrogen bonds, hydrophobic interactions, van der Waals forces, ionic interactions) responsible for maintaining protein structures.

Credit Hours - 2

This course focuses on the mechanisms, stereochemistry, and synthetic applications of reactions involving carbanions or potential carbanions with various carbonyl compounds. Key topics include:

Mechanisms:

• Formation of Carbanions: Understanding the conditions and reagents that favor carbanion formation.
• Reaction Pathways: Detailed study of the mechanisms through which carbanions react with carbonyl compounds, including nucleophilic addition and substitution reactions.

Stereochemistry:

• Stereochemical Outcomes: Analysis of the stereochemical outcomes of reactions involving carbanions.
• Chirality and Configuration: Understanding how carbanion reactions can create or influence chiral centers and the implications for the stereochemical configuration of products.

Synthetic Applications:

• Aldol Reactions: Utilizing carbanions in aldol reactions for the formation of β-hydroxy carbonyl compounds.
• Michael Additions: Applications of carbanions in Michael additions for the formation of 1,4-addition products.
• Enolate Chemistry: Use of enolates (a type of carbanion) in various synthetic transformations, including the formation of C-C bonds.
• Organometallic Reagents: Employing organometallic reagents (e.g., Grignard and organolithium reagents) in synthetic strategies involving carbanions.
• Carbonyl Compound Reactions: Comprehensive study of carbanion reactions with aldehydes, ketones, esters, amides, and other carbonyl-containing compounds.

Credit Hours - 2

This course explores the kinetic and stereochemical aspects of molecular rearrangement reactions, with a focus on the influence of neighboring groups. It covers rearrangements involving the migration of groups to both electron-deficient sites (carbon, nitrogen, oxygen) and electron-rich sites (carbon). Key topics include:

Kinetic Considerations:

• Reaction Rates: Factors affecting the rate of molecular rearrangements.
• Transition States: Understanding the transition states involved in rearrangement reactions.
• Neighboring Group Participation: Influence of neighboring groups on reaction pathways and stereochemical outcomes.

Stereochemical Considerations:

• Chirality and Stereoisomers: Analysis of how rearrangement reactions can affect the stereochemistry of molecules.
• Stereochemical Control: Strategies to control the stereochemistry in rearrangement reactions.

Types of Rearrangement Reactions:

• Electron-Deficient Sites: Rearrangements involving migration to carbon, nitrogen, and oxygen centers that are electron deficient.
• Electron-Rich Sites: Rearrangements involving migration to carbon centers that are electron rich.

Examples and Applications:

• Carbon Rearrangements: Detailed study of rearrangements involving migration to and from carbon centers.
• Nitrogen and Oxygen Rearrangements: Examination of rearrangements involving migration to nitrogen and oxygen centers.
• Synthetic Applications: Utility of rearrangement reactions in organic synthesis for the formation of complex molecules and functional groups.

Credit Hours - 6

BCMB 400 is a comprehensive research project that integrates biochemical principles with advanced analytical, cell biology, and molecular biology techniques. This course focuses on the development and execution of original research subjects, culminating in seminars and a thesis. Key aspects include:

Research Scope:

• Selection of Topics: Identifying original research subjects within the field of biochemistry and molecular biology.
• Literature Review: Conducting a thorough review of relevant literature to establish the background and rationale for the research project.

Experimental Design and Execution:

• Planning: Developing experimental methodologies and strategies.
• Execution: Performing laboratory work using biochemical and molecular techniques, as well as cell biology assays as required by the research question.

Data Analysis and Interpretation:

• Analytical Techniques: Utilizing advanced analytical methods for data collection.
• Interpretation: Analyzing and interpreting experimental results to draw meaningful conclusions.

Communication Skills:

• Seminars: Presenting research findings in seminars to peers and faculty.
• Thesis: Writing a comprehensive thesis that documents the research objectives, methodologies, results, and conclusions.

Credit Hours - 2

BCMB 408 focuses on the principles of entrepreneurship as applied to innovations in biosciences. The course covers fundamental aspects such as the nature and significance of entrepreneurship, with a specific emphasis on technology-based ventures in the biosciences sector. Topics include the characteristics of successful businesses driven by technology, assessment of technical and alternative risks, and the entrepreneurial decision-making process.

The course also explores creativity in generating business ideas, planning and developing products, and identifying resource needs. Alternative financing models and the importance of intellectual property protection, including patents, trademarks, and copyrights, are discussed in depth.

In the context of biosciences, the course examines innovations in medicine (including diagnostics and therapeutics), food and agriculture (focusing on quality, safety, efficiency of production, and processing), environmental applications (such as remediation, conservation, and restoration), and the development of value-added natural products.

Students engage with practical aspects of preparing for venture launch and managing growth and expansion in the biosciences sector, preparing them for entrepreneurial roles and innovation-driven careers within the field.

Credit Hours - 2

BCMB 412 provides a comprehensive exploration of molecular genetics, encompassing foundational concepts, chromatin and chromosome dynamics, genomics, genome maintenance, gene regulation in eukaryotes, and genetic manipulation in bacteria. Key topics include:

Genetic Foundations:

• Mendelian and Non-Mendelian Inheritance: Principles of inheritance and deviations from Mendelian genetics.
• Horizontal Gene Transfer: Mechanisms including transformation, transduction, and conjugation in bacteria.
• Recombination and Complementation: Genetic processes influencing variation and functional complementation.
• Mutational Analysis: Study of genetic mutations and their effects.
• Genetic Mapping and Linkage Analysis: Methods to map genes and analyze their linkage relationships.

Chromatin and Chromosomes:

• Karyotypes: Chromosomal arrangements and variations.
• Structural Aberrations: Translocations, inversions, deletions, and duplications impacting chromosome structure.
• Aneuploidy and Polyploidy: Abnormal chromosome numbers and their genetic implications.

Genomics:

• Genome Structure: Organization and composition of genomes.
• Physical Mapping: Techniques to map genes and genomic regions.
• Repeated DNA and Gene Families: Analysis of repetitive sequences and gene families.
• Gene Identification: Methods to identify genes within genomes.
• Transposable Elements: Mechanisms and impact of mobile genetic elements.

Genome Maintenance:

• DNA Replication: Processes and mechanisms ensuring accurate DNA duplication.
• DNA Damage and Repair: Cellular responses to DNA damage and repair mechanisms.
• DNA Modification: Epigenetic modifications influencing gene expression.
• DNA Recombination and Gene Conversion: Molecular mechanisms governing genetic exchange.

Gene Regulation in Eukaryotes:

• Cis-Acting Regulatory Elements: Elements influencing gene expression on the same chromosome.
• Trans-Acting Regulatory Factors: Factors controlling gene expression from distant locations.
• Gene Rearrangements and Amplifications: Structural changes affecting gene regulation.
• Large-Scale Genome Analysis: Overview of methodologies and outcomes from projects like the Human Genome Project.

Genetic Manipulation of Bacteria:

• Transposons and Plasmids: Tools for genetic manipulation and molecular cloning in bacteria.

Credit Hours - 2

BCMB 414 covers the intricate biochemical processes underlying plant metabolism, with a focus on nitrogen metabolism, secondary metabolites, photosynthesis, and molecular regulation in response to environmental stimuli. Key topics include:

Nitrogen Metabolism:

• Nitrogen Fixation: Mechanism involving dinitrogenase for converting atmospheric nitrogen into ammonia.
• Nitrogen Uptake and Reduction: Processes by which plants absorb and assimilate nitrogen for growth and development.

Secondary Metabolites:

• Terpenes: Biosynthesis via the mevalonic acid pathway and their roles in plant physiology.
• Phenolic Compounds: Synthesis through the shikimic acid pathway; functions in defense and signaling.
• Other Secondary Metabolites: Saponins, cardiac glycosides, cyanogenic glycosides, glucosinolates, and alkaloids; their biological functions and ecological roles.

Photosynthesis:

• Chloroplast Structure: Organization of chloroplasts for photosynthetic processes.
• Photoreceptors and Light Transduction: Mechanisms for converting light energy into chemical energy.
• Photosynthetic Electron Transport Chain: Flow of electrons through photosystems I and II.
• Carbon Fixation: Calvin cycle (C3), C2 and C4 cycles, and CAM metabolism; adaptations for efficient carbon assimilation under different environmental conditions.

Molecular and Biochemical Regulation:

• Environmental Cues: Responses to abiotic stresses (e.g., drought, temperature extremes) and biotic interactions (pathogens, symbiotic organisms).
• Regulation of Metabolic Pathways: Signaling pathways and gene expression modulation in response to environmental changes.
• Interaction with Pathogens and Symbiotic Organisms: Molecular mechanisms underlying plant defense and symbiotic relationships with microbes.

Credit Hours - 2

BCMB 416 explores the field of bioremediation, focusing on microbial genetics, microbial responses to environmental changes, biochemical cycling of essential elements, molecular mechanisms of biodegradation, and environmental applications. Key topics include:

Bacterial Genetics and Genomics:

• Review of genetic and genomic tools used in studying bacterial diversity and adaptation.

Microbial Diversity and Distribution:

• Exploration of microbial communities in various environmental settings and methods for their detection.

Microbial Responses to Environmental Changes:

• Mechanisms by which microbes respond to physical and chemical environmental stresses.
• Fine and coarse control of microbial responses, including morphological and genotypic changes.

Biochemical Cycling of Elements:

• Processes involving carbon, nitrogen, sulfur, iron, and mercury in microbial ecosystems.

Molecular Mechanisms:

• Biochemical pathways in microbes, including oxygenases and peroxidases involved in biodegradation.
• Microbial dechlorination reactions and their environmental significance.

Biodegradation:

• Breakdown of aromatic, aliphatic, chlorinated, and non-chlorinated hydrocarbons by microbial communities.
• Metabolism of polymers such as cellulose, xylan, and pectin by specialized microbial enzymes.

Environmental Applications:

• Utilization of bioremediation in replacing petroleum products, producing biofuels, and generating industrial bioproducts.

Prevention and Management of Environmental Contamination:

• Application of bioremediation techniques in sewage treatment, bio-leaching, and development of biodegradable materials.

Introduction to Phytoremediation:

• Overview of using plants to mitigate environmental pollution through natural processes.

Credit Hours - 2

BCMB 418 covers the specialized aspects of insect biochemistry and chemical ecology, highlighting the distinctive metabolic processes of insects, the role of hormones in growth and development, insect control strategies, and the intricate interactions between plants, insects, and their environment. Key topics include:

Distinctive Nature of Insect Metabolism:

• Energy Metabolism: Processes involved in energy synthesis, storage, mobilization, transport, and utilization, with a focus on flight metabolism.
• Regulatory Factors: Control mechanisms influencing metabolic activities in insects.

Insect Hormones Affecting Growth and Development:

• Biochemical Activities: Molecular actions of insect hormones in regulating growth, development, and metamorphosis.
• Insect Growth Regulators: Synthetic analogs and natural compounds influencing insect development.

Insect Control:

• Insecticides and Modes of Action: Mechanisms by which insecticides target physiological processes in insects.
• Detoxification Mechanisms: Enzymatic and biochemical pathways used by insects to detoxify xenobiotics.
• Insecticide Resistance: Molecular mechanisms and evolutionary aspects of resistance development.
• Synergists: Compounds enhancing the efficacy of insecticides.
• New Approaches to Insect Control: Innovative strategies integrating biological, chemical, and ecological principles.

Chemical Ecology:

• Plant Adaptation to Environment: Chemical responses of plants to environmental stresses and interactions with insects.
• Chemistry of Pollution: Impact of pollutants on plant-insect interactions and ecosystem dynamics.
• Plant-Insect Interactions: Mechanisms involving insect feeding stimulants, repellents, and plant defense chemistry.
• Animal-Animal Relationships: Communication through pheromones and chemical signaling.
• Plant-Plant and Plant-Microorganism Relationships: Chemical defenses, phytoalexins, and microbial interactions affecting plant health and insect interactions.

Credit Hours - 2

CHEM 374 provides an advanced exploration of analytical chemistry, encompassing classical methods, separation techniques, chromatography principles, spectrophotometry, and quality assurance protocols. Key topics include:

Classical Analytical Chemistry:

• Complexometric Titrations: Titrations involving the formation of complex ions for quantification.
• Non-Aqueous Solvent Titrations: Titration methods using solvents other than water.
• Gravimetric Methods: Techniques for determining the quantity of a substance based on its weight.

Separation Methods:

• Overview of techniques such as chromatography for separating mixtures based on different physical and chemical properties.

Principles of Chromatography:

• Fundamentals of chromatographic separation techniques, including gas chromatography (GC), liquid chromatography (LC), and high-performance liquid chromatography (HPLC).

Spectrophotometry:

• Principles and applications of spectrophotometric techniques for quantitative analysis based on absorption of light by substances.

Sampling and Evaluation of Analytical Data:

• Methods for collecting representative samples and statistical evaluation of analytical results.

Quality Assurance of Analytical Measurements:

• Procedures and protocols to ensure accuracy, precision, and reliability of analytical data.

Credit Hours - 2

To be done...