Syllabus & Course Curriculam
Course Type: MAJ-2
Semester: 2
Course Code: BBOTMAJ02C
Course Title: Cell Biology and Biochemical Basis of Life
(L-P-Tu): 4-2-0
Credit: 6
Practical/Theory: Combined
Course Objective: 1. To understand the structures and purposes of basic components of prokaryotic and eukaryotic cells, especially macromolecules, membranes, organelles, enzymes and bioenergetics. 2. To understand the chemical nature of biological macromolecules, their th
Learning Outcome: After the completion of the course the students will be able to: 1. Develop comprehensive understanding about the cellular architecture, communication systems and divisional types. 2. Understand details about bio-molecules, enzymes and bioenergetics. 3
(Theory, Credit 4)
Unit | Topic | No. of Lectures/Hrs |
1 | The Cell: Cell as a unit of structure and function; Characteristics of prokaryotic and eukaryotic cells; Origin of eukaryotic cell (Endosymbiotic theory).
| 2 |
2 | Cell wall and plasma membrane: Chemistry, structure and function of Plant cell wall. Overview of membrane function; fluid mosaic model; Chemical composition of membranes; Membrane transport – Passive, active and facilitated transport, endocytosis and exocytosis. Exracellular matrix.
| 5 |
3 | Cell organelles: Nucleus, Structure-nuclear envelope, nuclear pore complex, nuclear lamina, molecular organization of chromatin; nucleolus. Cytoskeleton: Role and structure of microtubules, microfilaments and intermediary filament. Chloroplast, mitochondria and peroxisomes: Structural organization; Function; Semi-autonomous nature of mitochondria and chloroplast. Endomembrane system: Endoplasmic Reticulum – Structure, targeting and insertion of proteins in the ER, protein folding, processing; Smooth ER and lipid synthesis, export of proteins and lipids; Golgi Apparatus – organization, protein glycosylation, protein sorting and export from Golgi Apparatus; Lysosomes.
| 15 |
4 | Cellular communication: General principles of cell communication, cell adhesion and roles of different adhesion molecules, gap junctions, extracellular matrix, integrins, neurotransmission and its regulation.
| 4 |
5 | Cell division: Phases of eukaryotic cell cycle, mitosis and meiosis; Regulation of cell cycle- checkpoints, role of protein kinases.
| 4 |
6 | Biomolecules: Types and significance of chemical bonds; Structure and properties of water; pH and buffers. Carbohydrates: Monosaccharides - structure of aldoses and ketoses, ring structure of sugars, conformations of sugars, mutarotation, anomers, epimers and enantiomers, structure of biologically important sugar derivatives, oxidation of sugars. Formation of disaccharides, reducing and non- reducing disaccharides. Polysaccharides – homo- and heteropolysaccharides, structural and storage polysaccharides. Lipids: Definition and major classes of storage and structural lipids; Fatty acids structure and functions; Essential fatty acids; Triacyl glycerols structure, functions and properties; Phosphoglycerides. Amino acids: Definition, classification & structures. Physico-chemical properties of amino acids (amphoteric molecules, ionisation, zwitterions, pk values, isoelectric point, Lambert-Beer’s law, optical density, absorption spectra). Proteins: Primary, secondary, tertiary and quaternary structure (definition and example), structure of globular protein (albumin, globulin, haemoglobin & myoglobin – Structure, function and occurrence in brief) and fibrous protein (keratin, collagen -role of Vitamin C in hydroxylation, Structure, function and occurrence in brief), Forces that stabilize structure of proteins, salting in and salting out, absorbance of proteins Nucleic acids: Nucleotides - structure and properties. Nucleic acid structure – Watson-Crick model of DNA. Structure of major species of RNA - mRNA, tRNA and rRNA. Nucleic acid chemistry - UV absorption, effect of acid and alkali on nucleic acids. Other functions of nucleotides – source of energy, component of coenzymes.
| 20 |
7 | Bioenergenetics: Laws of thermodynamics, concept of free energy, endergonic and exergonic reactions, coupled reactions, redox reactions. ATP: structure, its role as a energy currency molecule.
| 5 |
8 | Enzymes: Structure of enzyme: holoenzyme, apoenzyme, cofactors, coenzymes and prosthetic group; different classes of enzymes; Features of active site, substrate specificity, mechanism of action (activation energy, lock and key hypothesis, induced - fit theroy), Michaelis – Menten equation, enzyme inhibition and factors affecting enzyme activity. | 5 |
Practical (Credits -2, 60 Hrs)
Reading References:
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. Freeman and Company.
6. Karp, G. (2010). Cell Biology, John Wiley & Sons, U.S.A. 6th edition.
7. Hardin, J., Becker, G., Skliensmith, L.J. (2012). Becker’s World of the Cell, Pearson Education Inc. U.S.A. 8th edition.
8. Cooper, G.M. and Hausman, R.E. (2009) The Cell: A Molecular Approach. 5th edition. ASM Press & Sunderland, Washington, D.C.; Sinauer Associates, MA.
9. Becker, W.M., Kleinsmith, L.J., Hardin. J. and Bertoni, G. P. (2009) The World of the Cell. 7th edition. Pearson Benjamin Cummings Publishing, San Francisco.
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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