BIOCHEMISTRY AND ENZYMOLOGY

Paper Code: 
MBL 122
Credits: 
5
Contact Hours: 
75
Objective: 

Course Outcomes (COs):

               Course Outcomes

Learning and teaching strategies

Assessment Strategies

  
 

Upon completion of the course the learner will:

CO 6: Understand the basic principles of bioenergetics, thermodynamics and redox reactions.

CO 7: Classify amino acids on the basis of functional groups and apply in building protein structure and folding.

CO 8: Understand the principles of protein purification and formulate a method for purification of a specific protein.

CO 9: Classify carbohydrates and lipids on the basis of structure and function.

CO 10: Understand metabolism of carbohydrates and lipid and compute the ATP production.

CO 11: Understand Enzyme kinetics and apply to  enzyme engineering.

Interactive Lectures,

Discussion,

Tutorials,

Demonstrations,

Assignments

Reading Journals

Class test, Semester end examinations, Quiz, Solving problems in tutorials, Assignments, Presentation, Individual and group projects

  

 

15.00
Unit I: 
Chemical foundations of Biology
  • pH, pK, acids, bases, buffers, chemical bonds, Bioenergetics: Principles of thermodynamics: free energy, important energy rich molecules, standard free energy change, concept of redox reactions.
  •  Principles of self-assembly, Hierarchy of molecular organization of living systems.
15.00
Unit II: 
Amino acids and proteins
  • Amino acids – structure and functional group properties, peptides and structural organization of proteins- primary, secondary, tertiary and quaternary structure, structure-function relationships in model proteins like ribonuclease A, myoglobin, hemoglobin, chymotrypsin etc.
  • Elucidation of primary and higher order structures, Ramachandran plot.
  • Protein folding: Anfinsen’s Dogma, Levinthal paradox, cooperativity in protein folding, free energy landscape of protein folding and pathways of protein folding, molten globule state, chaperons, diseases associated with protein folding, introduction to molecular dynamic simulation.
  • Basic principles of protein purification; tools to characterize expressed proteins
15.00
Unit III: 
Carbohydrates
  • Classification and structural features of carbohydrates- mono, di, oligo and polysaccharides; Isomerization: epimer, anomer and mutarotation. Metabolism of carbohydrates, main sources of carbohydrates, enzymatic conversion and mobilization as glucoses or fructoses, roles of epinephrine and glucagon and insulin in glycogen metabolism, glycolysis, Krebs cycle, terminal oxidation/ oxidative phosphorylation, mechanism of ATP synthesis, rate controlling steps and regulation.
15.00
Unit IV: 
Lipids
  • Classification, Structure and functions.  Metabolism of Lipid and fat bodies: Beta-oxidation and channeling of the products to ATP production, minor pathway of fatty acid oxidation (alpha and omega oxidation), Biosynthesis of saturated and unsaturated fatty acids, Ketone bodies, membrane lipids-cholesterol, phospholipid and glycolipid; biosynthesis of fat soluble vitamins; biosynthesis of Eicosanoids (prostaglandin, leukotrienes and thromboxane).
15.00
Unit V: 
Enzymes

·         Kinetics: Rate of reactions, specific activity, molecular activity, Km, Kcat, Michaelis- Menten and Line weaver Burk plot, enzyme inhibition, mechanism of enzyme catalysis (acid-base electrostatic, metal ion, free radicals, transition state binding and covalent catalysis, proximity and orientation effects, contribution of strain.

 Factors affecting enzyme activity, enzyme inhibition. Allosteric enzymes and bi-substrate reactions. Rationale for modification of enzyme function, Enzyme Engineering: modification of structure and catalytic properties of enzymes

ESSENTIAL READINGS: 
  • Biochemistry, D. Voet and J.G. Voet, John Wiley & Sons, (3rd Edition), 2004.
  • Principles of Biochemistry, Lehninger, Nelson and Cox, (8th Edition), 2021.
  • Principles and Techniques in Biochemistry and Molecular Biology, Edited by Keith Wilson and John Walker, Cambridge University Press, (8th Edition), 2018.
  • Instant Notes- Biochemistry (1st Indian Edition), B.D. Hames and N.M. Hooper, Viva Books Pvt, Ltd., 2001.

 

REFERENCES: 

SUGGESTED READINGS:

  • Biochemistry and Molecular Biology by W.H. Elliot and Daphne C. Elliot, Oxford University Press, (3rd Edition), 2005.
  • Physical Biochemistry, D Friefelder, W.H. Freeman & Company, 17th Reprint, 1999.
  • Understanding Chemistry, CNR Rao, University Press, Hyderabad 1999.
  • Essentials of Molecular Biology, David Friefelder, Jones and Barllett Publications, 7th Reprint, 2001.

e RESOURCES:

  • Dobson, C. M. (2003). Protein Folding and Misfolding. Nature, 426(6968), 884-890. doi:10.1038/nature02261. 5.
  • Richards, F. M. (1991). The Protein Folding Problem. Scientific American, 264(1), 54-63. doi:10.1038/scientificamerican0191-54.

JOURNALS

Academic Year: 
2022-2023
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