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Unit-1
Introduction to proteins
Introduction to peptides and proteins. Structural and functional diversity. Classification of proteins - simple and conjugated proteins; monomeric and multimeric proteins.
Unit-2
Hierarchy of protein structure organization
Organization of protein structure into primary, secondary, tertiary and quaternary structures. Force stabilizing the protein structure - covalent (disulfide bridges) and non-covalent (electrostatic interactions and salt bridges, hydrophobic, hydrogen bonding, van der Waals). The peptide bod, dihedral angles psi and phi, helices, sheets, turns and loops, Ramachandran map. Motifs and domains. Structural proteins- alpha-keratin, silk fibroin, collagen. Globular and fibrous proteins, membrane proteins.
Unit-3
Protein sequencing and Databases
Sequencing techniques- N-terminal and C-terminal amino acid analysis, Edman degradation. generation of overlap peptides using different enzymes and chemical reagents. Disulfide bonds and their location. Solid phase peptide synthesis. Protein databases-sequence and structural based.
Unit-4
Protein folding and Conformational Disease
denaturation and renaturation of ribonuclease A- discovery of protein folding. Introduction to thermodynamics of protein folding. Assisted folding by molecular chaperones, chaperonins and PDI. Disease associated with protein misfolding- Alzheimer's and Creutzfeldt-Jakob disease.
Unit-5
Specialized proteins
Transport proteins: myoglobin and hemoglobin- oxygen binding curves, influence of 2,3-BPG, CO2 and H+; Cooperativity between subunits and models to explain the phenomena- concerted and sequential models. Hemoglobin disorders- Sickle cell anemia
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