GROUP-39 B.Sc. Micrology Jobs

GROUP-39 B.Sc. Micrology Jobs 1) General awareness, Reasoning, Mathematics, Science, History including Haryana related history, current affairs, literature, Geography, Civics, Environment, Culture etc.- (Weightage 20%) 2) Computer terminology, Fundamentals, word software, excel software, Power point, internet, web browsing, Communication, emails, downloading and uploading data on websites etc. - (Weightage 10%) 3) Subject related syllabus-

(Weightage 70%) -------------------------------------------------------------------------------------------------------------------------------------- Structure and Function of Biomolecules Water and Carbohydrates: Water and its physicochemical properties; Classification of carbohydrates; Occurrence, characteristics, structure and functions of monosaccharides, disaccharides, oligosaccharides and polysaccharides; structure and conformation of sugars; monosaccharides: stereoisomerism and optical isomerism; chemical reactions of the functional groups; sugar derivatives; Glycoproteins; peptidoglycan, proteoglycan, N-linked and O-linked glycoproteins bacterial cell wall polysaccharides; blood group polysaccharides; glycobiology, glycol-mics Amino acids and nucleotides: Structure, nomenclature, classification, acid-base properties of amino acids and their applications, chemical reactions of amino acids; stereoisomerism and optical properties of amino acids; non-natural amino acids; Structure and properties of purines and pyrimidine bases; structure and functions of nucleotides. Lipids: Classification of lipids; structures, nomenclature and properties of fatty acids; structure, properties and functions of acylglycerols, plasmalogens, phospholipids, sphingolipids, glycolipids, steroids, prostaglandins and eicosanoids, bile acids lipoamino acids; chemical composition and biological role of lipoproteins; structure and functions of fat-soluble vitamins. Hormones: General characteristics, classification, chemistry and functions of thyroid, parathyroid, adrenal, pancreatic, gastric and reproductive hormones; hypothalamus and pituitary; detection of hormones; hormone replacement therapy; pheromones. Cell Biology Prokaryotic and eukaryotic cells, Common and distinguishing features between them. Plasma membrane: An overview of membrane functions; Brief history of studies on plasma membrane structure, chemical composition of membranes: membrane lipids, membrane carbohydrates and membrane proteins, Glycocalyx, membrane lipids and membrane fluidity, the dynamic nature of the plasma membrane, methods of introducing a membrane-impermeable substance into a cell. Membrane transport of small molecules: Principles of membrane transport, Passive diffusion, facilitated diffusion and carrier proteins, ion channels, active transport driven by ATP hydrolysis and by ion gradients Mitochondria: Mitochondrial structure and function, mechanism of oxidative phosphorylation, critical roles of mitochondria in cell metabolism besides ATP production Chloroplast and other plastids: structure of chloroplast, role of chloroplasts in photo-synthetic metabolism, different types of plastids Peroxisomes: structure and functions of peroxisomes and their involvement in photorespiration. Cell wall: bacterial and eukaryotic cell wall Endoplasmic reticulum: ER and protein secretion, targeting proteins to the ER, insertion of proteins into the ER membrane, protein folding and processing in the ER, SER and lipid synthesis Golgi-apparatus: Organization of the Golgi-complex, protein glycosylation within the Golgi, lipid and polysaccharide metabolism in the Golgi

Lysosomes: Major characteristics and its role in intra-cellular digestion. The Cytoskeleton: Micro-filaments: structure and organization, muscle contractility; Microtubules: structure and dynamic organization of microtubules, Microtubule organizing centres: centrosomes and basal bodies; Microtubule motor proteins; Cilia and flagella: structure and functions, Intermediate filaments: intermediate filament proteins; assembly, intracellular organization and functions of intermediate filaments Cellular interactions: Extracellular matrix: matrix structural proteins, matrix polysaccharides, matrix adhesion proteins, Interactions of cells with extracellular materials: integrins, focal adhesions and hemidesmosomes; Interactions of cells with other cells: Adhesion junctions, Tight junctions, Gap junctions and Plasmodesmata. Nucleus: Nuclear envelope and traffic between the nucleus and the cytoplasm, structure of the nuclear envelope, nuclear pore complex, Organization of Nucleolus The Cell cycle: Overview of eukaryotic cell cycle, Regulation of cell cycle by cell growth and extracellular signals, cell cycle checkpoints, Regulators of cell cycle progression: protein kinases and cell cycle regulation, families of cyclins and cyclin-dependent kinases, DNA damage check points Cell death and cell renewal: Apoptosis (Programmed cell death), caspases: the executioners of apoptosis, central regulators of apoptosis: TheBcl-2family; Stem cells and their properties, medical applications of adult stem cells, embryonic stem cells and therapeutic cloning. Proteins and Proteomics Primary structure of proteins: An overview of protein structure; hierarchy of protein structure; Ramachandran plot; Determination of primary structure of protein - determination of N and C-terminal residue; Determination of amino acid composition of protein and determination of sulfhydryl groups; location of disulphide bonds; Chemical synthesis of peptides; Structure and function of some biologically important polypeptides. Secondary and tertiary structure of proteins: Alpha helix and beta structure; Collagen helix and other types of helical structures; Super secondary structures; Amino acid sequence and three-dimensional structure; Domains; Forces stabilizing the secondary and tertiary structure Sequencing, protein folding and denaturation: Protein sequencing; Sequenators; Quaternary structure of protein; Structure and function of haemoglobin and cytochrome c; Denaturation and renaturation of proteins; Characteristics of molten globule state; Proteins involved in folding; Models of protein folding; Chaperones and Levinthal paradox; Protein conformation and diseases. Protein purification and separation techniques: Protein purification; criteria of purity, and fold purification; Ion-exchange, gel-filtration and affinity chromatography techniques; High performance liquid chromatography (HPLC); Iso-electric focusing (IEF); Native-PAGE and SDS-PAGE; Detection and quantification of proteins in gels; Recovery of proteins from gels. Proteomics: Overview and tools; Two-dimensional PAGE; Protein spot detection; Mass spectrometry: matrix assisted laser desorption ionization MS, Electrospray ionization MS, and tandem MS for protein identification; Identification of protein-protein interactions; Protein complexes; X-ray crystallography; Transmembrane domains; Functional proteomics; Application of proteome analysis. Bioenergetics and Metabolism-I Bioenergetics: Concept of Free energy; standard Free energy; Relationship between standard free- energy change and equilibrium constant; Coupled reactions; High-energy compounds. Biological oxidation: Oxidation & reduction; Oxidation-reduction half reactions; Nernst equation, measurement of standard reduction potentials; Calculation of Delta-G from standard reduction potentials; Enzymes involved in oxidation and reduction (oxidases, dehydrogenases, hydroperoxidases and oxygenase's). Introduction to Metabolism and Experimental approaches for studying metabolism. Carbohydrate Metabolism: Reactions, energetics and regulation of glycolysis; Feeder pathways for glycolysis; Fate of pyruvate under aerobic and anaerobic conditions; Pasteur effect; Pyruvate dehydrogenase complex and its regulation; Reactions, regulation and amphibolic nature of TCA Cycle; Anaplerotic reactions; Glyoxylate cycle; Pentose Phosphate Pathway; Gluconeogenesis; Cori cycle; Biosynthesis of lactose and sucrose; Glycogenesis and Glycogenolysis; Control of glycogen metabolism; Maintenance of blood glucose levels.

Lipid Metabolism: Mobilization and hydrolysis of triacylglycerols; Fatty acid oxidation: Franz Knoop's experiment; β-oxidation of saturated, unsaturated and odd-chain fatty acids; Peroxisomal β-oxidation; Minor pathways of fatty acid oxidation (α- and ω- oxidations); Formation and utilization of Ketone bodies; Biosynthesis of saturated fatty acids; Elongation and desaturation of fatty acids; Biosynthesis of triacylglycerols; Regulation of fatty acid metabolism; Cholesterol biosynthesis and its regulation; Biosynthesis of glycerophospholipids and sphingolipids; Breakdown of sphingolipids by lysosomal enzymes; Formation of prostaglandins, prostacyclin's, thromboxane's and leukotrienes from arachidonic acid. Mitochondrial Electron Transport Chain and Oxidative Phosphorylation: Mitochondrial Transport Systems; Nature, order and organization of the components of electron transport chain; electron flow from NADH and FADH2 to O2; sites of ATP production; inhibitors of electron transport chain; Coupling between oxidation and phosphorylation; Chemiosmotic hypothesis of oxidative phosphorylation; Mechanism of ATP synthesis: Structure of proton-translocating ATP synthase; Binding Change Mechanism for proton-driven ATP synthesis; Uncoupling of oxidative phosphorylation; Control of oxidative phosphorylation. Metabolism-II Amino acid degradation: General reactions of amino acid metabolism: Transamination; Oxidative, non- oxidative deamination and decarboxylation reactions; Role of glutamine in ammonia transport; Glucose- Alanine Cycle; Urea Cycle; Metabolic breakdown of individual amino acids (both essential and non- essential) Amino acid biosynthesis: Biosynthesis of non-essential and essential amino acids; Regulation of amino acid biosynthesis; Amino acids as biosynthetic precursors of phosphocreatine, glutathione, dopamine, non-epinephrin and epinephrin, GABA, histamine, serotonin, polyamines (spermine and spermidine), and indole-3-acetic acid. Porphyrins: Structure of porphyrins; Important porphyrins occurring in nature; Biosynthesis of heme and its regulation; Degradation of heme; Regulation of hemebiosynthesis; Chlorophyll biosynthesis. Nucleotide metabolism: De novo biosynthesis and regulation of purine and pyrimidine nucleotides; Salvage pathways of purines and pyrimidines; Ribonucleotide reductase and formation of deoxyribonucleotides (dNTPs) from ribonucleotides (NTPs); Catabolism of purine and pyrimidine nucleotides; Chemotherapeutic agents as inhibitors of enzymes in nucleotide biosynthetic pathways; Biosynthesis of nicotinamide coenzymes, flavin coenzymes and coenzyme A. Integration of metabolism: basic strategy of catabolic metabolism; Recurring motifs in metabolic regulation; Major metabolic pathways and control sites; Key junctions in metabolism (glucose-6-phosphate, pyruvate and acetyl CoA); Organ specific metabolic profile; Metabolic changes induced by food intake and starvation; Ethanol metabolism in the liver. Secondary plant metabolism: Primary and secondary metabolites; Isoprenoids: introduction, different classes with examples; biosynthesis of carotenoids (Limonene, Lycopene and β-Carotene); Alkaloids: definition, classification according to their heterocycles with examples; physiologically active alkaloids (used in medicine and plant chemical defence); Phenylpropanoids: Introduction; overview of products of the phenylpropanoid metabolism; Biosynthesis of lignin; Flavonoids: nature; classification of aglycons with examples; functions of flavonoids; Nature of Tannins, Cyanogenic glycosides and Glycosylates Clinical Biochemistry Clinicalbio-chemistryandqualityassurance:biologicalsamples(blood,urineandcerebrospinalfluid):chemical composition, collection,processing, storage and reservation;Qualitycontrol:accuracy, precision, Specificity, Sensitivity, Levy Jining's chart. Blood: clinical significance and functions of plasma proteins (albumin, alpha 1-antitrypsin, haptoglobin, caeruloplasmin, transferrin, C-reactive protein); Disorders of haemoglobin: thalassemia, anaemia (different types) and porphyria's. Clinical enzymology: Enzymes as diagnostic tool; Clinically important enzymes: alkaline phosphatase, acid phosphatase, aldolase, creatine kinase, LDH, AST, ALT, lipase, amylase and 5'-nucleotidase; isoenzymes and their diagnostic importance. Organ function tests: Assessment of liver, kidney, exocrine pancreas and G.I. tract function tests. Detoxification: Phase I and Phase II reactions.

Metabolicdisorders:Disordersofcarbohydratemetabolism:Diabetesmellitus, diabetic ketoacidosis,hypoglycemia,glycogenstorage disease and galactosemia; glucose tolerance test; disorders of lipid: Refsum's disease, fatty liver and lipotropic factors, hypo lipoproteinemia and hyper lipidaemia. Atheros sclerosis: pathogenesis and risk factors; Disorder of amino acid metabolism: Maple syrup urine disease, phenylketonuria, Alkaptonuria, cystinuria and homocystinuria; disorder of nucleic acid metabolism: Gout, Lesch-Nyhan Syndrome, Hypouricemia, Oro tic Aciduria; disorders of calcium, magnesium, phosphorous, iron, copper and selenium metabolism; disorders of fat soluble (A, D, E and K) and water soluble vitamins (Thiamine, riboflavin, niacin, pyridoxine, pantothenic acid, biotin, folic acid, vitamin B12 and ascorbic acid) Hormone disturbances: disturbances related to protein hormones (anterior and posterior pituitary), steroid hormones and thyroid hormones. Electrolyte and acid base balance: disorders of electrolytes (hypernatremia, hyponatremia, hypokalaemia, hyperkalaemia, hyperchloremia, hypochloraemia); water and acid base balance (metabolic and respiratory acidosis, metabolic and respiratory alkalosis) Neuropsychiatric disorders: Alzheimer's & Parkinson's disease. Enzymology Introduction: Historical perspectives; General characteristics; Nomenclature and classification; Introduction to the following terms with examples - Holoenzyme, apoenzyme, cofactors, coenzymes, prosthetic groups, metalloenzymes, turnover number, enzyme activity units, and specific activity.Multienzyme systems and multifunctional enzymes with specific examples and significance. Enzyme specificity: Types of specificity; three-point attachment theory to explain stereospecificity; Lock- and-key hypothesis; Induced- fit hypothesis; Hypothesis involving strain or transition-state stabilization.Enzyme Catalysis: Role of NAD+/NADP+, FMN/FAD, coenzyme A, thiamine pyrophosphate, pyridoxal phosphate, lipoic acid, biocytin, Vitamin B12 Coenzyme, and tetrahydrofolate coenzymes in enzyme catalysis; Common features of active sites;Reactionco-ordinate diagram; Proximity & orientation, acid-base catalysis, and covalent catalysis; Mechanism of action of chymotrypsin, ribonuclease, carboxypeptidase, and lysozyme Enzyme assay: Introduction; Kinetic and coupled enzyme assays. Enzyme Kinetics: Factors affecting enzyme activity; Arrhenius plot; Derivation of Michaelis-Menten equation for uni-substrate reactions; Km and its significance; Kcat/Km and its importance; Measurement of Km and Vmax by Lineweaver-Burk plot and other linear transformations of MM equation; Bi-substrate reactions: Sequential and ping-pong mechanisms with examples and determination of Km and Vmax for each substrate (derivations excluded); Use of initial velocity studies, product-inhibition studies and isotope exchange at equilibrium for determining the kinetic mechanism of a bi-substrate reaction. Methods of studying fast reactions: A brief account of rapid mixing techniques, flash photolysis and relaxation methods. Enzyme inhibition: Reversible (competitive, non- competitive, and uncompetitive) and irreversible (affinity labels and suicide inhibitors) enzyme inhibitors; Determination of Ki. Investigation of active site structure: Methods for identification of binding and catalytic sites- Trapping the enzyme-substrate complex, use of substrate analogues, chemical modification of amino acid side chains in enzymes, enzyme modification by proteases and effect of changing pH. Enzyme regulation: Coarse and fine control of enzyme activity; Enzyme induction & Repression; Feedback inhibition; Allosteric enzymes with aspartate trans-carboxylase as an example; Concerted and sequential models for action of allosteric enzymes; Negative and Positive Cooperativity; Hill plot; Scat chard plot; Regulation by reversible and irreversible covalent modification of enzymes; Isoenzymes. Ribozyme and Abzyme Molecular Biology-1 Basic Concepts of Genetic Information: Nucleic acids as the genetic material - experimental evidences; Chargaff's rules Structure of DNA, Structural polymorphism of DNA (A, B and Z-DNA) various forces responsible for stability of DNA, DNA topology, topological and geometric properties, DNA supercoiling, Topoisomerases in prokaryotes and eukaryotes, DNA organization in prokaryotes and eukaryotes, C- value paradox, denaturation: different ways for carrying out denaturation, renaturation: requirements, kinetics, significance, various classes of DNA: highly repetitive, moderately repetitive and unique sequence, RNA: structure and types.

DNA replication, mutations and DNA repair: Possible modes of DNA replication, Meselson-Stahl experiment, DNA polymerases and other enzymes involved in DNA replication, Okazaki fragments, Mechanism of replication in prokaryotes and eukaryotes, inhibitors of DNA replication, molecular basis of mutations, DNA repair mechanisms like direct, base-excision, nucleotide-excision, mismatch, SOS and recombinational repair. Transcription and post-transcriptional modifications: RNA polymerase/s in prokaryotes and eukaryotes, DNA footprinting technique, initiation, elongation and termination of transcription in prokaryotes and eukaryotes, inhibitors of transcription, RNA replicase, reverse transcriptase, post-transcriptional modifications: different types of introns and their splicing mechanisms, processing of mRNA, rRNA and tRNA precursors, overlapping genes and split genes. Protein synthesis, targeting and degradation: Characteristics of the genetic code, biological significance of degeneracy, decoding the code, Wobble hypothesis, ribosomes structure and function in prokaryotes and eukaryotes, Aminoacyl tRNA-synthetases, various factors and steps involved in protein synthesis in prokaryotes and eukaryotes, polyribosomes, post-translational processing, signal hypothesis and protein targeting to lysosomes, Plasma membrane, extracellular matrix and different compartment of mitochondria and chloroplast, protein degradation. Food Biochemistry Classes and sources of nutrients (overview), energy value of foods, Basal metabolic rate, specific dynamic action, nutritional importanceofcarbohydrates, Glycaemic index,fibresinnutrition,nutritionalimportanceoflipids,essentialfattyacids,nutritional importance of proteins, nitrogen balance, mutual supplementation of proteins, concept of balanced diet, Vitamins:majorfunctions,dietarysources,deficiencysymptomsof fat-soluble and water-soluble vitamins,hypervitaminosisof fat-soluble vitamins; Minerals: major functions, dietary sources, deficiency symptoms and toxicity symptoms of major and trace minerals Food toxicity and safety: Microbial contamination, environmental contamination, natural toxins, agricultural residues, intentional food additives. Applications of major enzymes in food industry Nutritional disorders:Lipoproteins and cardiovascular disease: 'good' and 'bad' cholesterol, risk factors for cardiovascular disease. Nutrition and Cancer: Associations between nutritional factors and common cancer sites; effect of different foods, beverages, physical parameters and other additional factors on cancer. Molecular Biology - II Gene regulation: Various levels of control of gene expression in prokaryotes and eukaryotes, operon concept, regulation of expression