Course Details
Subject {L-T-P / C} : BM6438 : Biophysics and Structural Biology { 3-0-0 / 3}
Subject Nature : Theory
Coordinator : Prof. Subhankar Paul
Syllabus
Three dimensional conformations of proteins, Ramachandran plot, motifs, folds, mechanism of protein folding, fibrous proteins, membrane proteins and their structures. Hydrogen bonding, hydrophobic interactions, ionic interactions, disulphide bonds and their role in protein structure. Secondary structural elements and organisation of tertiary structure. Helix-coil transition and zipper model Principles of Nucleic acid structures : Nucleic acid structure and composition, supercoiling of DNA, denaturation and renaturation kinetics, nucleotide sequence composition: unique, middle and highly repetitive DNA Methods of determination of biomolecular structures: Macromolecular structure determination: X-ray crystallography, optical, UV and IR spectroscopy, luminescence, fluorescence, magnetic resonance and electron microscopy Biomolecular interactions : ProteinProtein interactions, protein-carbohydrate interactions, Protein-DNA interactions. General features and thermodynamic aspects of protein folding, Detection of folding intermediates, Complex and folding kinetics.
Course Objectives
- To understand the sructure and function of proteins.
- To learn about protein folding in vivo and in vitro
- To learn about protein conformation change and monitoring through various methods
- To learn how to determine the three domensional structure of globular proteins.
Course Outcomes
On completion of this course, the student will be able to: <br />1. Understand the evolution of protein structural motifs and domains and associate this with function <br />2. Use on-line structural databases and tools to predict the properties, structure and function of proteins. <br />3. Understand and explain enzyme mechanisms in a structural context. <br />4. Describe mechanisms of protein folding and the roles of natively unstructured proteins in biology. <br />5. Understand how cross-talk between proteins and post-translational protein modifications (e.g. phosphorylation, ubiquitination) facilitate information processing in cells.
Essential Reading
- . D. L. Nelson and M. M. Cox, Lehninger, Principles of Biochemistry, W. H. Freeman,, Prentice Hall , Fourth Edition, 2004
- K. EvanHolde, C. Johnson and P. S. Ho,, Principles of Physical Biochemistry, Prentice Hall, Second Edition, 2005, Prentice Hall , Second edition, 2005
Supplementary Reading
- P R. Bergethon, The Physical Basis of Biochemistry, The Foundations of Molecular Biophysics, Springer , Corrected edition, 2000
- K. EvanHolde, C. Johnson and P. S. Ho,, Principles of Physical Biochemistry, Prentice Hall, Second Edition, 2005, Prentice Hall , Second edition, 2005