JNTUK B.Tech Structural Biology gives you detail information of Structural Biology R13 syllabus It will be help full to understand you complete curriculum of the year.
UNIT I: INTRODUCTION
Levels of structures in Biological macromolecules, the chirality of biomolecules, proteins, nucleic acids, carbohydrates and lipids, cofactors, vitamins and hormones. Forces that determine Protein and Nucleic acid structure, basic problems. Polypeptide chains; geometric, potential energy calculations, observed values for rotation angles, hydrogen bonding, hydrophobic interactions and water structures; ionic interactions, disulphide bonds. The introduction of structural biology
LO: To understand the basics of structural biology
LA: Assessment by the ability to differentiate the properties and types of polymers.
UNIT II: PROTEIN FOLDING
Types of proteins and interactions that govern protein folding, protein structure, The protein globule and hydrophilic interactions organized folds, folding mechanisms, membrane proteins, helix-coil transitions,
LO: To demonstrate the protein folding and protein structure.
LA: Assessment by testing of protein interactions computationally.
UNIT III: BIOMOLECULAR INTERACTIONS
Molecular recognition, supramolecular interactions, Functional importance of Protein and protein- nucleic acid interactions. Specific and non- specific DNA- protein complexes and their importance.
LO: To understand the biomolecular interactions.
LA: Assessment by evaluating the interactions of specific molecules.
UNIT IV: STRUCTURAL ANALYSIS OF MACROMOLECULES
Prediction of protein structure; Sequence-structure relationships, Nucleic acids; general characteristics of nucleic acid structure, geometric, glycosidic bond rotational isomers backbone rotational isomers and ribose puckering forces stabilizing ordered forms, base pairing, base stacking, tertiary structure of nucleic acids.
LO: To demonstrate the structural analysis of macromolecules.
LA: Assessment by analyzing and differentiating the structures of macromolecules.
UNIT V: KINETICS OF LIGAND INTERACTIONS:
Biochemical Kinetics studies, uni- molecular reactions, simple bimolecular multiple intermediates, steady state kinetics, catalytic efficiency relaxation spectrometry, ribonuclease as an example.
LO: To understand the kinetics of ligand interactions.
LA: Assessment by the ability to derive the kinetics of ligand interactions.
UNIT VI: TECHNIQUES FOR THE STUDY OF BIOLOGICAL STRUCTURE & FUNCTION
Size and shape of micro molecules: photons, chromophores, transition dipole moments, absorbance, and concentration. circular dichroism: molecular chirality and structural transitions of macromolecules, methods of direct visualization macromolecules as hydrodynamic particles – macromolecular diffusion ultracentrifugation viscometry. X- ray crystallography; determination of molecular structures, X- ray fiber diffraction electron microscopy; neutron scattering – light scattering, NMR spectroscopy.
LO: To demonstrate techniques for the study of biological structure & function
LA: Assessment by using these techniques for analysis of structure for specific molecule.
TEXT BOOK
- Tinoco. I Jr, Sauer. K, Wang. J. C & Puglisi, J. D. Physical Chemistry: Principles and Applications in Biological Sciences, 4thedition, Prentice Hall, 2001.
REFERENCES
- A.M. Lesk Introduction to Protein Architecture, 1st edition, Oxford University Press, 2001.
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