Q11
NAT • 1M
Biochemistry, Microbiology & Molecular Biology
Phylum proteobacteria is subdivided into -, -, -, - and -proteobacteria based on (A) G+C content (B) 23S rRNA sequences (C)tRNA sequences (D)16S rRNA sequences 2013 BIOTECHNOLOGY - BT BT 5/13
Q26
NAT • 1M
Cellular & Applied Biotechnology
Match the commercial microbial sources in Group I with the products in Group II. Group I Group II P. Corynebacteriumlilium 1. 2,3-Butane di-ol Q. Klebsiellaoxytoca 2. Poly- β-hydroxybutyric acid R. Aspergillusniger 3. Glutamic acid S. Alcaligeneseutrophus 4. Citric acid (A) P-3,Q-1,R-2,S-4 (B) P-3,Q-1,R-4,S-2 (C) P-1,Q-3,R-2,S-4 (D) P-1,Q-3,R-4,S-2
Q27
NAT • 1M
Bioprocess Engineering
Match the entries in the Group I with the elution conditions in Group II. Group I Group II P. Ion-exchange chromatography 1. Isocratic solvent Q. Hydrophobic column chromatography 2. Ampholytes R. Gel filtration chromatography 3. Increasing gradient of salt S. Chromatofocusing 4. Decreasing gradient of polarity (A) P-4,Q-1,R-2,S-3 (B) P-4,Q-3,R-1,S-2 (C) P-3,Q-4,R-1,S-2 (D) P-3,Q-4,R-2,S-1 2013 BIOTECHNOLOGY - BT BT 7/13
Q29
NAT • 1M
Biochemistry, Microbiology & Molecular Biology
Match the cell structures in Group I with the organismsin Group II. Group I Group II P. Endospores 1. Methanobacterium Q. Bipolar flagella 2. Treponema R. Pseudomurine in cell wall 3. Spirillum S. Periplasmic flagella 4. Clostridium (A) P-4, Q-3, R-1, S-2 (B) P-4, Q-3, R-2, S-1 (C) P-3, Q-4, R-1, S-2 (D) P-4, Q-1, R-3, S-2
Q30
NAT • 1M
Biochemistry, Microbiology & Molecular Biology
Match the antibioticsinGroup Iwith the targets inGroup II. Group I Group II P. Sulfonamide 1. Peptidoglycan synthesis Q. Quinolones 2. Peptide chain elongation R. Erythromycin 3. Folic acid biosynthesis S. Cephalosporin 4. Topoisomerase (A) P-3, Q-4, R-1, S-2 (B) P-2, Q-4, R-3, S-1 (C) P-4, Q-1, R-2, S-3 (D) P-3, Q-4, R-2, S-1
Q32
NAT • 1M
Biochemistry, Microbiology & Molecular Biology
Match the entries inGroup I with the enzymes inGroup II. Group I Group II P. NAD+ 1. Glutathione peroxidase Q. Selenium 2. Nitrogenase R. Pyridoxal phosphate 3. Lactate dehydrogenase S. Molybdenum 4. Glycogen phosphorylase (A) P-3, Q-2, R-4, S-1 (B) P-4, Q-1, R-3, S-2 (C) P-3, Q-1, R-4, S-2 (D) P-3, Q-4, R-2, S-1 2013 BIOTECHNOLOGY - BT BT 8/13
Q33
NAT • 1M
Biochemistry, Microbiology & Molecular Biology
Match the herbicides in Group Iwith the target enzymesin Group II. Group I Group II P. Glyphosate 1. Nitrilase Q. Bromoxynil 2. Acetolactatesynthetase R. Sulphonylureas 3. Dehalogenase S. Dalapon 4. 5-Enolpyruvyl shikimate3-phosphate synthase (A) P-4, Q-1, R-2, S-3 (B) P-2, Q-1, R-4, S-3 (C) P-4, Q-3, R-2, S-1 (D) P-3, Q-2, R-4, S-1
Q35
NAT • 1M
Biochemistry, Microbiology & Molecular Biology
Match the entries in Group Iwith the entries in Group II. Group I Group II P. RNAse P 1. Polyadenylation Q. RNase H 2. Splicing R. snRNAs 3. Ribozymes S. CstF 4. DNA-RNAhybrids (A) P-3, Q-4, R-2, S-1 (B) P-4, Q-3, R-2, S-1 (C) P-3, Q-2, R-1, S-4 (D) P-2, Q-4, R-1, S-3
Q37
NAT • 2M
Biochemistry, Microbiology & Molecular Biology
Match the entries in the Group Iwith the entries inGroup II. Group I Group II P. Threading 1. Gene duplication Q. FASTA 2. Fold prediction R. Profile 3. HMM S. Paralogs 4. k-tuple (A) P-2, Q-1, R-3, S-4 (B) P-2, Q-4, R-3, S-1 (C) P-3, Q-4, R-2, S-1 (D) P-1, Q-4, R-3, S-2
Q42
NAT • 2M
Recombinant DNA Technology
A complete restriction digestion of a circular plasmid (5000bp) was carried out with HindIII,BamHIandEcoRIindividually. Restriction digestion yielded following fragments. Plasmid + HindIII→ 1200bp and3800bp Plasmid + BamHI→5000bp Plasmid + EcoRI→ 2500bp The number of sites for EcoRI,BamHIandHindIIIpresent on this plasmid are (A)EcoRI-2, BamHI-1, HindIII-2 (B) EcoRI-1, BamHI-1, HindIII-2 (C)EcoRI-3, BamHI-2, HindIII-1 (D) EcoRI-2, BamHI-2, HindIII-1 2013 BIOTECHNOLOGY - BT BT 10/13 Q. 43 - Q. 47 are of numerical answer type.
Q47
NAT • 2M
Biochemistry, Microbiology & Molecular Biology
A fed batch culture was operated with intermittent addition of glucose solution at a flow rate of 200 ml h-1. The values of K s, m and D are 0.3 g l -1, 0.4 h-1 and 0.1 h-1, respectively. Determine the concentration of growth limiting substrate (gl-1) in the reactor at quasi-steady state. ____________ Common Data Questions Common Data for Questions 48 and 49: A solution was prepared by dissolving 100 mg of protein X in 100 ml of water. Molecular weight of protein X is 15,000 Da; Avogadro's number = 6.022x 10 23.
Q49
NAT • 2M
Biochemistry, Microbiology & Molecular Biology
The number of moleculespresent in this solution is (A) 40.15x10 19 (B) 6.023 x1019 (C)4.015 x1019 (D) 0.08 x1019 2013 BIOTECHNOLOGY - BT BT 11/13 Common Data for Questions 50 and 51: The binding efficiency of three different receptorsR1 , R2 and R3 were tested against a ligand using equilibrium dialysis, with a constant concentration of receptor and varying concen trations of ligand. The Scatchard plot of receptor titration with different concentration of ligand is given below (ris moles of bound ligand per moles of receptor and c is concentration of free ligand) 12 4 3 2 1 r/c R1 R2 R3 r R4 30
Q61
NAT • 2M
Biochemistry, Microbiology & Molecular Biology
Velocity of an object fired directly in upward direction is given by ݐwhere ݐtime) is in seconds. When will the velocity be between 32 m/sec and 64 m/sec? (A) (1, 3/2) (B) (1/2, 1) (C) (1/2, 3/2) (D) (1, 3)