Syllabus & Course Curriculam
Course Type: MAJ-3
Semester: 3
Course Code: BMCBMAJ03T
Course Title: BIOCHEMISTRY (THEORY)
(L-P-Tu): 4-2-0
Credit: 6
Practical/Theory: Combined
Course Objective: 1. To learn about the structural and functional role of vital biomolecules like carbohydrates, proteins, fats, and nucleic acids in biological system 2. To study the bioenergetics and enzyme kinetics.
Learning Outcome: After completing this course, the students will be able to – 1. Understand the chemistry of carbohydrates and its classification. 2. Understand the chemistry of amino acids and hierarchy of protein structure – primary, secondary, tertiary and quatern
SEMESTER III
MAJOR COURSE 01
COURSE TITLE: BIOCHEMISTRY (THEORY)
TOTAL HOURS: 60 CREDITS: 4
Unit 1. BioenergeticsNo. of hours:8
First and second laws of Thermodynamics. Definitions of Gibb’s Free Energy, enthalpy, and Entropy and mathematical relationship among them, Standard free energy change and equilibrium constant, high energy bond, biological applications of thermodynamics.
Unit 2. Carbohydrates No. of hours:10
Families of monosaccharides: aldoses and ketoses, trioses, tetroses, pentoses, and hexoses. Stereoisomerism of monosaccharides, epimers, Mutarotation and anomers of glucose. Furanose and pyranose forms of glucose and fructose, Haworth projection formulae for glucose; chair and boat forms of glucose, muramic acid, N-acetyl neuraminic acid. Disaccharides; concept of reducing and non-reducing sugars, occurrence and Haworth projections of maltose, lactose, and sucrose, Polysaccharides, storage polysaccharides, starch and glycogen. Structural Polysaccharides, cellulose and chitin, reactions of carbohydrates.
Unit 3. Structures of DNA and RNA/Genetic Material No. of hours:8
DNA Structure: Miescher to Watson and Crick-historic perspective (1 lecture) DNA structure, Salient features of double helix, Types of DNA. Types of genetic material, denaturation and renaturation, cot curves. DNA topology–linking number, topoisomerases. Organelle DNA- mitochondria and chloroplast DNA.
Unit 4. Lipids No. of hours:10
Definition and major classes of storage and structural lipids. Storage lipids. Fatty acid’s structure and functions. Essential fatty acids. Triacylglycerols structure, functions and properties. Saponification Structural lipids. Phosphoglycerides: Building blocks, General Structure functions and properties. Structure of phosphatidyl ethanol amine and Phosphatidyl choline, Sphingolipids: building blocks, structure of sphingosine, Special. mention of sphingomyelins, cerebrosides and gangliosides Lipid functions: cell signals, cofactors, prostaglandins, Introduction of lipid micelles, monolayers, bilayers.
Unit 5. Amino Acids and Proteins No. of hours :10
Functions of proteins, Primary structures of proteins: Amino acids, the building blocks of proteins, General formula of amino acid and concept of zwitterion. Titration curve of Amino acid and its Significance.
Classification, biochemical structure of Amino acids, Ninhydrin reaction. Non protein amino acids: Gramicidin, beta-alanine, D alanine and D-glutamic acid.
Secondary structure of proteins: Peptide unit and its salient features. The alpha helix, the beta pleated sheet and their occurrence in proteins, Tertiary and quaternary structures of proteins. Forces holding the polypeptide together. Human haemoglobin structure.
Unit 6. Enzymes: No. of hours :10
Structure of enzyme: Apoenzyme and cofactors, prosthetic group-TPP, Coenzyme NAD, metal cofactors, Classification of enzymes, Mechanism of action of enzymes: active site, transition state complex and activation energy. Lock and key hypothesis, and Induced Fit hypothesis.
Significance of hyperbolic, double reciprocal plots of enzyme activity, Km and allosteric mechanism Definition soft Terms–enzyme unit, specific activity and turnover number, Multi enzyme complex: pyruvate dehydrogenase; isozyme: lactate dehydrogenase, Effect of pH and temperature on. Enzyme activity. Enzyme inhibition: competitive, non-competitive and mixed inhibition.
Unit 7. Vitamins No. of hours: 4
Classification and characteristics with suitable examples, sources and importance.
1. Campbell, MK (2012) Biochemistry, 7th ed., Published by Cengage Learning
2. Campbell, PN and Smith AD (2011) Biochemistry Illustrated, 4th ed., Published by Churchill Livingstone
3. Tymoczko JL, Berg JM and Stryer L (2012) Biochemistry: A short course, 2nd ed., W.H.Freeman
4. Berg JM, Tymoczko JL and Stryer L (2011) Biochemistry, W.H.Freeman and Company
5. Nelson DL and Cox MM (2008) Lehninger Principles of Biochemistry, 5th Edition., W.H. Freemanand Company,
6. Willey MJ, Sherwood, LM &Woolverton C J (2013) Prescott, Harley and Klein’s Microbiologyby. 9th Ed., McGrawHill
7. Voet,D. and Voet J.G (2004) Biochemistry 3rd edition, John Wiley and Sons
COURSE TITLE: BIOCHEMISTRY(PRACTICAL) CREDITS : 2
Biochemical Estimation: DNA (DPA Method), RNA (Orcinol Method), Sugar (DNSA Method), Amino Acid (Ninhydrin Method) and Protein (Lowry’s Method).
Basic Features
Undergraduate degree programmes of either 3 or 4-year duration, with multiple entry and exit points and re-entry options, with appropriate certifications such as:
Note: The eligibility condition of doing the UG degree (Honours with Research) is- minimum75% marks to be obtained in the first six semesters.
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