Introductory Biochemistry - Syllabus
Paper Code
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212903
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Marks: 100
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Credits: 4
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Class Hours: 60
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Paper Title:
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Introductory Biochemistry
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1.
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History,
scope and future of biochemistry
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2.
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Concept
of life and living process. The
identifying characteristics of a living matter.
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3.
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The
cell and its evolution, from molecules to the first cell, from .prokaryotes
to eukaryotes, structure and function of sub-cellular organelles, their
isolation and identification, brief treatment of meiosis and mitosis.
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4.
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Biomolecules:
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(i)
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Carbohydrates
: Biological functions of carbohydrates,
classification and nomenclature, optical properties, ring structure of common
monosaccharides, proof of ring structure of glucose, mutarotation of glucose,
general .properties and colour test of reducing sugars, important derivatives
of monosaccharides, sugar acids.
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Disaccharides:
Maltose, lactose, sucrose and other
disaccharides, isolation from natural source, structure and biological
importance.
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Polysaccharides:
Storage and structural polysaccharides,
structures and functions of starch, glycogen and cellulose, other
polysaccharides of biological interests: structure and their functions.
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(ii)
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Lipids: nomenclature, classification, general reactions of fats,
fatty acids, and sterols, structure and biological functions of different
classes of lipids, isolation of cholesterol and .phospholipids from natural
sources.
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(iii)
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Amino
acids and peptides: Structural features, optical
activity, classification, physio-chemical properties of amino acids and
peptides.
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(iv)
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Proteins:
General introduction to .proteins,
classification of proteins based on biological functions, shape and
structure, isolation, and purification, primary structure of proteins, sequence
determination of insulin, sequence homology of homologous proteins,
denaturation of proteins.
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Fibrous
proteins: Secondary structure of
proteins, protein conformation, alpha-keratins, X-ray analysis of keratin,
planar peptide bonds, alpha-helix, helix forming and destablizing amino
acids, the insolubility of alpha-keratins, beta-keratins – conformation and
structure, structures of collagen and elastin, filamentous proteins – actin,
myosin and microtubules.
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Globular
proteins: Tertiary structures of
proteins: distinctive tertiary structures of myoglobin, and ribonuclease,
renaturation of unfolded and denatured ribonuclease, factors maintaining the
tertiary structure of globular proteins, oxygen-binding curves of haemoglobin
and myoglobin, the cooperative binding of oxygen by haemoglobin, factors
contributing to oxygen saturation curve of hemoglobin, sickle-cell anaemia
and its relation to haemoglobin.
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Protein
purification and characterization :
Dialysis and ultrafiltration, density gradient centrifugation, gel
filtration, isoelectric .precipitation, solvent fractionation, salting-in and
salting-out of proteins, electrophoresis, ion-exchange chromatography,
selective adsorption, affinity chromatography, minimum molecular weight
determination.
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Books
Recommended:
- Lehninger Principle of Biochemistry
By: David L., Nelson and Michael M. Cox.
Publisher: W.H. Freeman and Company, New
York
- Biochemistry
By:
Lubert Stryer
Publisher: W.H. Freeman and Company, New
York
- Biochemistry
By: Donald Voit and Juldith Voit
Publisher:
John Wiliy & Sons.
- Cell and Molecular Biology
By: Gerald Karp
Publisher: John Willy & Sons