Enzymes Before they can react, many molecules need to be destabilized. This state is typically achieved through the input of a small amount of activation energy changing the reaction from a biosynthetic to a catabolic pathway changing the three-dimensional shape of the molecule oxidizing the molecules by removing electrons the input of a small amount of activation energy changing the reaction from a biosynthetic to a catabolic pathway changing the three-dimensional shape of the molecule oxidizing the molecules by removing electrons ANSWER DOWNLOAD EXAMIANS APP
Enzymes Tryprotophan synthetase of E.coli, a typical bifunctional oligomeric enzyme consist of a protein designated A a protein designated B two proteins designated A and B a protein A and one-subunit a a protein designated A a protein designated B two proteins designated A and B a protein A and one-subunit a ANSWER DOWNLOAD EXAMIANS APP
Enzymes Which of the following (s) is/are serine proteases? Elastase Trypsin all of these Chymotrypsin Elastase Trypsin all of these Chymotrypsin ANSWER DOWNLOAD EXAMIANS APP
Enzymes Which of the following is false statement with regard to comparison between Serine and HIV proteases? Both show specificity for certain amino acid sequences Both require water to complete the catalytic cycle Both use nucleophilic attack to hydrolyze the peptide bond Both forms an acyl-enzyme intermediate Both show specificity for certain amino acid sequences Both require water to complete the catalytic cycle Both use nucleophilic attack to hydrolyze the peptide bond Both forms an acyl-enzyme intermediate ANSWER DOWNLOAD EXAMIANS APP
Enzymes The nucleophile in serine proteases is water Serine Asparagine both (a) and (b) water Serine Asparagine both (a) and (b) ANSWER DOWNLOAD EXAMIANS APP
Enzymes The proteolysis rate enhancement by chymotrypsin (~1010 folds) corresponds to a reduction in activation energy of about 88 kJ/mol 49 kJ/mol 40 kJ/mol 58 kJ/mol 88 kJ/mol 49 kJ/mol 40 kJ/mol 58 kJ/mol ANSWER DOWNLOAD EXAMIANS APP
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