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Students will be able to
•Understand the structures and purposes of basic components of prokaryotic and eukaryotic cells, especially macromolecules, membranes, and organelles.
•Exploration of different types of biomolecules and the importance in cellular composition
•Carry out a range of laboratory exercises, demonstrating the development of practical scientific skills.
•Know about the structure and functions of macromolecules and the major organelles that occur in eukaryotic cells.
•Students will be exposed to the history of Biochemistry and key contributions of scientists.
•They will study the properties of carbohydrates, proteins, lipids,cholesterol, DNA, RNA, glycoproteins and glycolipids and their importance in biological systems.
•They will understand the methods of determination of amino acid and nucleotide sequence of proteins and DNA respectively.
Module-I Carbohydrates: Definition, empirical formulae, classification, biological importance.Monosaccharides: Configuration relationship of D-aldoses, D-ketoses. General properties of aldoses and ketoses. Oxidation, reduction, reducing property, formation of glycosides, acylation, methylation, condensation – phenyl hydrazine, addition – HCN. Inter-conversion of aldoses and ketoses by chemical method. Ascending and descending the series by chemical methods. Stereochemistry of monosaccharides, (+) and (-), D and L, epimers, anomers, and diastereoisomers. Structure and biological importance of amino sugars, deoxy sugars, sugar acids, neuraminic and muramic acid.
Module-II Disaccharides:Establishment of structures of sucrose and lactose, biological importance and structure of isomaltose, trehalose and maltose.
Polysaccharides: Partial structure, occurrence and importance of starch, glycogen, inulin, cellulose, chitin, and pectin.Glycosaminoglycans: Occurrence, importance and the structure of the repeating units of heparin, hyaluronic acid, teichoic acid and chondroitin sulphate. Bacterial cell wall polysaccharide, peptidoglycans.
Module-III Amino acids: Structure and classification of amino acids based on polarity. Reactions of the amino groups with HNO2, LiAlH4, ninhydrin, phenyl isothiocyante, dansylchloride, flurodinitrobenzene. Zwitterionic properties. Pka values. Reaction of carboxyl group – Hydrazine. Any method for the chemical synthesis of amino acids D & L notation. Peptides: Peptide bond, structure and biological importance of glutathione, valinomycin, leuenkaphelin, synthetic peptides- polyglutamic acid, polylysine. Chemicalsynthesis of dipeptides.
Module -IV Proteins: Isolation, methods of purification-dialysis salting out, pH precipitation and solventprecipitation. Classification of proteins based on solubility, structure and functions with examples. Primary Structure of proteins, methods of determining N- and C- terminal aminoacids, amino acid composition.Sequencing by Edman’s degradation method. Secondary Structure – α Helix. β-sheet, β-bend. Tertiary of myoglobin and quaternary structure of hemoglobin, denaturation and renaturation of proteins. Anfinsen’s experiment.
Module-V Lipids:Classification and biological role. Fatty acids – Nomenclature of saturated and unsaturated fatty acids. Physiological properties of fatty acids. Acylglycerols:Mono, di and triglycerols. Saponification, saponification value, iodine value, acid value and significance.
Module-VI Phosphoglycerides:Structure of lecithin, cephalins, phosphotidylinosital, plasmalogens, and cardiolipin. Biological role of phosphoglycerides. Sphingolipids: Structure and importance of sphingomyelin., Glycosphingolipids: Structure and importance of gangliosides and cerebrosides. Eicosanoids: Structure of PGE2, and PGF2α importance of prostaglandins. Biological roles of thromboxane, leukotrienes and prostaglandins.
Module-VII Nucleic acids:Isolation of DNA and RNA. Composition of DNA. Nucleosides and nucleotides. Chargaff’s rule. Watson and Crick model of DNA. Melting of DNA (Tm). RNA:Composition, types (mRNA, tRNAandrRNA), secondary structures of tRNA – clover leaf model. Chemical reactions of RNA and DNA with acid and alkali, colour reactions of DNA and RNA.
• Qualitative analysis of biomolecules
• Carbohydrates –Molisch, Benedict’s / Fehling’s, picric acid, Barfoed’s, Bial’s, Seliwanoff’s,
• Glucose, fructose, lactose, maltose and sucrose.
• Proteins – Precipitation reactions of proteins, colour reactions of proteins, colour reactions of
amino acids like tryptophan, tyrosine, cysteine, methionine, arginine, proline and histidine.
• Colour reactions of proteins – Biuret, xanthoproteic, Millon’s.
• Lipids– solubility, acrolein test, Salkowski test, Lieberman-Burchard test.
• Qualitative tests for nucleic acid.
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.
Dr Sitaram Swain has received PhD degree from Utkal University in the year 2017. He is also trained and experienced from TATA Memorial Hospital, Mumbai, India. He has experienced with cell line culture, clinical biochemistry, immuno-fixation, immunoassay, cancer cytogenetic, serum protein electrophoresis and tumour marker analysis. He has qualified NET(ICAR-ASRB) in Animal biotechnology. He has […]