Syllabus

Module 1: Protein Structure and Folding Mechanisms
Three-dimensional conformations of proteins, including the Ramachandran plot, motifs, folds, and the mechanism of protein folding. Structural features of fibrous and membrane proteins and the role of interactions such as hydrogen bonding, hydrophobic interactions, ionic interactions, and disulfide bonds in stabilizing protein structure. Secondary structural elements, the organization of tertiary structures, helix-coil transitions, and the zipper model are also discussed.
Module 2: Principles of Nucleic Acid Structures
Focuses on the structure and composition of nucleic acids, exploring DNA supercoiling, denaturation, and renaturation kinetics, and nucleotide sequence composition, including unique, middle, and highly repetitive DNA sequences.
Module 3: Biomolecular Structure Determination Techniques
Introduction to techniques for determining macromolecular structures, including X-ray crystallography, optical spectroscopy, UV and IR spectroscopy, luminescence, fluorescence, magnetic resonance, and electron microscopy. Structural analysis of biomolecules.
Module 4: Biomolecular Interactions
Explores the various interactions between biomolecules, including protein-protein, protein-carbohydrate, and protein-DNA interactions. It emphasizes the importance of these interactions in biological processes and their structural implications.
Module 5: Thermodynamics and Kinetics of Protein Folding
The general features and thermodynamic aspects of protein folding, detection of folding intermediates, and the complex kinetics associated with protein folding. It provides insights into the principles governing folding mechanisms and stability.

To understand the structure and function of bio molecules.

To learn about protein, its conformation and various methods to monitoring its folding

To learn about protein, Nucleic acid and their structure and composition

To learn how to determine the three domensional structure of globular proteins.

On completion of this course, the student will be able to:
1. Understand the evolution of protein structural motifs and domains and associate this with function
2. Use on-line structural databases and tools to predict the properties, structure and function of proteins.
3. Understand and explain enzyme mechanisms in a structural context.
4. Describe mechanisms of protein folding and the roles of natively unstructured proteins in biology.
5. Understand how cross-talk between proteins and post-translational protein modifications (e.g. phosphorylation, ubiquitination) facilitate information processing in cells.

. 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

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