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MSRIT Structural Biology Sem 5
No Units Titles Sub Titles Chapters
1 Unit 1 Introduction to structural biology Scope and importance, Levels of molecular organization, atom-to-cell-to-organism, Hierarchy related to size, molecular weight and complexity of biopolymers, Structure of water, properties of electrolytes, pH and its biological significance, Chirality of Biological molecules, Brief discussion on, primary structure and role of amino acids, proteins, nucleic acids, carbohydrates, lipids, cofactors, vitamins, and hormones VIEW CHAPTERS
2 Unit 2 Structural characteristics of proteins Conformational analysis and forces that determine protein structures, polypeptide chain geometries, phi, psi, omega angles, Secondary structures, Ramachandran or steric contour diagram, allowed chi angles of side chains in proteins, hydrogen bonding, disulphide bonds, hydrophobic interactions, alpha helices, beta sheets, General features and thermodynamic aspects of protein folding, folding kinetics, cooperative interactions, allosteric effects, Relationship between the primary, secondary, and tertiary structure of proteins, Antibodies and antigens interactions, fibrous proteins (structure of collagen, keratin), Quaternary structures, Homo & hetero, dimers, trimers and tetramers, Protein folds, proteinprotein/ ligand interactions VIEW CHAPTERS
3 Unit 3 Structure of nucleic acids and biomembranes General characteristics of nucleic acid structures (A, T, G, C, U), geometries, glycosidic bond, rotational isomers, Stabilizing ordered forms of DNA (A, B and Z), base pairing types, base stacking, tertiary structure of DNA and preferred torsion angles, Intra-molecular interactions, Melting of the DNA double helix (Hyperchromicity), denaturation, renaturation, Ribose puckering and tertiary structure of tRNA, Protein nucleic acid interaction, Structure and conformational properties of cell membranes (Singer and Nicholson model), Integral proteins in membranes, conformational variations during ion transport, monitoring membrane potentials VIEW CHAPTERS
4 Unit 4 Biophysical Techniques Optical Activity, Optical rotator dispersion (ORD), Circular dichroism (CD), applications, Sedimentation, Principle, Svedberg co-efficient, Ultracentrifuge and its applications, Spectro-fluorimetry & its applications, Light Scattering, principles of Static and dynamical light scattering, Zimm plot and its applications, Mass spectrometry, Principle, instrumentation, Surface plasmon resonance (SPR), Matrix-assisted laser desorption/ionization-Time-of-flight (MALDI-TOF), Electron spin resonance (ESR), Principle, Instrumentation, Spin labeling studies and its applications VIEW CHAPTERS
5 Unit 5 Biomolecular structure and dynamics Structure determination methopds, X-ray crystallography, protein crystal growth methods, x-ray diffraction, single crystal and fibre diffraction techniques of data collection, Phase problem, Phase determination methods, Patterson, direct, molecular replacement and anomalous dispersion, structure validation, 1-D, 2-D, NMR, Nuclear Overhauser effect, COSY, NOESY, Biomolecular Interactions and Dynamics VIEW CHAPTERS
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