PROTEIN STRUCTURE, FUNCTION AND ENGINEERING




UNIT I BONDS AND ENERGIES IN PROTEIN MAKEUP 12
Covalent, ionic, hydrogen, coordinate, hydrophobic and vander walls interaction in protein
structure – Interaction with electromagnetic radiation (radio, micro, infrared, visible,
ultraviolet, X-ray) and elucidation of protein structure.
UNIT II AMINO ACIDS AND THEIR CHARACTERSTICS 12
Amino acids and their molecular properties – Chemical reactivity in relation to posttranslational
modification (involving amino, carboxyl, hydroxyl, thiol, imidazole groups) and
peptide synthesis.
UNIT III PROTEIN ARCHITECTURE 12
Primary structure – Peptide mapping, peptide sequencing – Automated edman method and
mass-specs – High-throughput protein sequencing setup – Secondary structure – Alpha, beta
and loop structures and methods to determine – Super-secondary structure – Alpha-turnalpha,
beta-turn-beta (hairpin), beta-sheets, alpha-beta-alpha, topology diagrams, up and
down and TIM barrel structures nucleotide binding folds, prediction of substrate binding sites
– Tertiary structure – Domains, folding, denaturation and renaturation – Overview of
methods to determine 3D structures – Quaternary structure – Modular nature, formation of
complexes.
UNIT IV STRUCTURE-FUNCTION RELATIONSHIP 12
DNA-binding proteins – Prokaryotic transcription factors – Helix-turn-Helix motif in DNA
binding – Trp repressor – Eukaryotic transcription factors – Zn fingers – Helix-turn-helix
motifs in homeodomain – Leucine Zippers – Membrane proteins – Genera characteristics –
Trans-membrane segmenta – Prediction – Bacteriorhodopsin and photosynthetic reaction
center – Immunoglobulins – IgG Light chain and heavy chain architechture – Abzymes and
Enzymes – Serine proteases – Understanding catalytic design by engineering trypsin,
chymotrypsin and elastase – Substrate-assisted catalysis other commercial applications.
UNIT V PROTEIN ENGINEERING 12
Advantages and purpose – Overview of methods – Underlying principles with specific
examples: thermal stability T4-lysozyme – Recombinant insulin to reduce aggregation and
inactivation, de novo protein design.
Total: 60
TEXT BOOK
1. Branden, C. and Tooze J., “Introduction to Protein Structures”, 2nd Edition, Garland
Publishing, 1999.
REFERENCES
1. Primrose, S.B. and Twymann R.H., “Protein Folding, Evolution and Design”, 2001.
2. Voet, D. and Voet ,G., “Biochemistry”, 3rd Edition, John wiley and Sons, 2001.


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