Enzymes The proteolysis rate enhancement by chymotrypsin (~1010 folds) corresponds to a reduction in activation energy of about 40 kJ/mol 58 kJ/mol 88 kJ/mol 49 kJ/mol 40 kJ/mol 58 kJ/mol 88 kJ/mol 49 kJ/mol ANSWER DOWNLOAD EXAMIANS APP
Enzymes The cleavage specificity of trypsin and chymotrypsin depend in part on the proximity of Ser 195 to the active site or specificity pocket size, shape, and charge of the active site or specificity pocket absence of water in the active site presence of a low-barrier hydrogen bond in the active site or specificity pocket proximity of Ser 195 to the active site or specificity pocket size, shape, and charge of the active site or specificity pocket absence of water in the active site presence of a low-barrier hydrogen bond in the active site or specificity pocket ANSWER DOWNLOAD EXAMIANS APP
Enzymes The role of Asp 102 and His 57 during trypsin catalysis is to clamp the substrate into the active site function as a proton shuttle keep the specificity pocket open neutralize the charge on the other's side chain clamp the substrate into the active site function as a proton shuttle keep the specificity pocket open neutralize the charge on the other's side chain ANSWER DOWNLOAD EXAMIANS APP
Enzymes Common feature in all serine proteases is a cluster of reactive serine residues hydrophilic specificity pocket hydrophobic specificity pocket single reactive serine residue cluster of reactive serine residues hydrophilic specificity pocket hydrophobic specificity pocket single reactive serine residue ANSWER DOWNLOAD EXAMIANS APP
Enzymes Which of the following is false statement with regard to comparison between Serine and HIV proteases? Both use nucleophilic attack to hydrolyze the peptide bond Both show specificity for certain amino acid sequences Both forms an acyl-enzyme intermediate Both require water to complete the catalytic cycle Both use nucleophilic attack to hydrolyze the peptide bond Both show specificity for certain amino acid sequences Both forms an acyl-enzyme intermediate Both require water to complete the catalytic cycle ANSWER DOWNLOAD EXAMIANS APP
Enzymes Tryprotophan synthetase of E.coli, a typical bifunctional oligomeric enzyme consist of a protein A and one-subunit a a protein designated B a protein designated A two proteins designated A and B a protein A and one-subunit a a protein designated B a protein designated A two proteins designated A and B ANSWER DOWNLOAD EXAMIANS APP
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