BCMB 401: PROTEIN CHEMISTRY I

Primary structure: amino acid composition of proteins, determination of amino acid sequence, importance of primary structure synthesis of peptides, covalent modification of polypeptides.

Secondary structure (regular arrangement of the polypeptide backbone): peptide bond and its structural implications; random polymers; Ramachandran Plot.  Regular conformation of polypeptides; -helix, -pleated sheets, other helices (3₁₀-  helix), super-secondary structures (coiled-coil -helix).  Examples: fibrous proteins; -keratins, silk fibroin, collagen.

Tertiary structure (folded conformation of globular proteins): determination of protein structure by X-ray crystallography, evidence for folding, reverse turns (-turns) super-secondary structures (motifs), domains, interiors and exteriors, unfolding and folding.  Example:  Myoglobin.

Quaternary structure (aggregation of globular proteins).  Example: haemoglobin. 

Physical forces responsible for maintaining structure.