Which of the following protease enzymes is correctly identified with its specifi

Question

Which of the following protease enzymes is correctly identified with its specificity ? Trypsin: cleaves on C -side of acidic amino acids chymotrypsin: cleaves on C-side of aliphatic amino acids staphylococcal protease: cleaves on C-side of acidic ammo acids clostripain: cleaves on C-side of lysine none of the above are correct Amino acid side chains capable of forming hydrogen bonds are usually located on the protein___and form hydrogen bonds primarily with the____. surface, water solvent interior, water solvent surface, other amino acid side chains interior, other amino acid side chains all are true A hydrophobic interaction might occur with in a protein between which of the following amino acid pairs? Ser/lle Val/Leu Tyr/Cys Lys/Asn His/Val Secondary and higher orders of structure are determined by all EXCEPT: hydrophobic interactions. ionic bonds. van der Waals forces. hydrogen bonds peptide bonds. If an aspartic acid residue were present in the interior of a globular protein, it would most likely be_____. deprotonated and thus negatively charged tightly associated with the R-group of a lysine residue react with a cysteine to form a thioester react with a serine to form an ester none of the above Planarity of the peptide bond means that no rotation occurs about the ____bond while rotation is allowed about the___ and___bonds. C(O)-N; C alpha-C beta; N-C alpha C(O)-N; C alpha-C(O); N-C alpha C alpha-C(O); C(O)-N; N-C alpha N-C alpha; C alpha-C(O); C(O)-N none of the above A Ramachandran plot shows. the amino acid residues which have the greatest degree of rotational freedom. the sterically allowed rotational angles between R groups and a-carbons in a peptide the sterically allowed rotational angles between C_alpha and the amino nitrogen (C_alpha N) as well as between C_alpha and the amide carbonyl carbon (C_alpha-CO). the sterically allowed rotational angles about the amide nitrogen (NH) and C the amino acid residues that form a-helix, beta-sheet, etc. Alpha helices are stabilized primarily by; hydrogen bonds between the main chain peptide bond component atoms.

Explanation / Answer

32Q. ANSWER IS C

Trypsin cleaves peptides on the C-terminal side of lysine and arginine amino acid residues.

chymotrypsin prefers large hydrophobic residues. Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids.

Staphylococcal protease has a unique specificity for cleaving peptide bonds on the carbonyl side of aspartic or glutamic acid residues.

Clostripain is a proteinase that cleaves proteins on the carboxyl peptide bond of arginine

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