#Question id: 12945
#Unit 13. Methods in Biology
#Question id: 10384
#Unit 6. System Physiology – Plant
Nitrogenase enzyme complex catalyzes the molecular nitrogen fixation, this enzyme not only fixes nitrogen but also perform other reactions given below. Which one is not performed by nitrogenase?
#Question id: 2189
#Unit 2. Cellular Organization
Which of the following is not true of membrane phosphoglycerides?
#Question id: 4272
#Unit 3. Fundamental Processes
There are two classes of release factors for translation termination. Choose correct statements
A. Class I release factors recognize the stop codons and trigger hydrolysis of the peptide chain from the tRNA in the P-site.
B. Prokaryotes have two class I release factors called RF1 and RF2. RF1 recognizes the stop codon UGA, UAA and RF2 recognizes the stop codon UAG and UAA.
C. In eukaryotic cells, there is a single class I release factor called eRF1 that recognizes all three stop codons.
D. Class II release factors stimulate the dissociation of the ribosome after release of the polypeptide chain.
#Question id: 879
#Unit 1. Molecules and their Interaction Relevant to Biology
Correct approaches to protein structure prediction-:
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i. Homology modeling |
a) Methods is the Rosetta program, formulated by David Baker. To satisfy the program’s computational needs, a volunteer network of ∼100,000 computers, known as Rosetta@home, provides the 500,000 or so hours of processing time required to generate a structure. |
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ii. Structural genomics |
b) which seeks to determine the X-ray structures of all representative domains, is aimed at expanding this predictive technique. The identification of structural homology is likely to provide clues as to a protein’s function even with imperfect structure prediction. |
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iii. Threading |
c) Is a computational technique that attempts to determine the unknown structure of a protein by ascertaining whether it is consistent with a known protein structure. It does so by placing the unknown protein’s residues along the backbone of a known protein structure and then determining whether the amino acid side chains of the unknown protein are stable in that arrangement |
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iv. Ab initio |
d) Aligns the sequence of interest with the sequence of a homologous protein or domain of known structure—compensating for amino acid substitutions, insertions, and deletions—through modeling and energy minimization calculations. |