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 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.