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Protein Structure

Enzymatic cleavage for protein determination

QuestionAnswer
Trypsin Lysine (K), Arginine (R) - C terminus
Chymotrypsin Tyrosine (Y), Tryptophan (W), Phenylalanine (F), Leucine (L ) - C terminus
Thermolysin Isoleucine (I), Valine (V) - N terminus
Pepsin Tyrosine (Y), Tryptophan (W), Phenylalanine (F), others - N terminus
Staph. aureus (V8 Protease) Glutamate (E), Asparatate (D) - C terminus
Myobacter protease Lysine (K) - N terminus
Papain Arginine (R), Lysine (K) - fast C terminus; Glutamic acid (Q), Histidine (H), Glycine (G), Tyrosine (Y) - slow C terminus
Subtilism Glutamine (Q), Serine (S), Leucine (L), Tyrosine (Y), Phenylalanine (F) - C terminus
Pronase Many
Lys C Lysine (K) - C terminus
Arg C Arginine (R) - C terminus
Carboxypeptidase A Non-polar residues
Carboxypeptidase B Lysine (K) and Arginine (R)
Carboxypeptidase C All residues at different rates
Carboxypeptidase Y Hydrophobic (faster), hydrophilic (slower)
Dipeptidyl aminopeptidase Dipeptides
Leucine aminopeptidase Preferentially hydrophobic
Aminopeptidase M Broader specificity
Met-X Cyanogen Bromide
Arg-X Trypsin (also cleaves lysine)
Glu(E)-X S. aureus V8 protease (also cleaves Asp (D))
Try(W)-X BNPS
Lys(K)-X Endo Lys C Protease
Arg(R)-X Endo Arg C Protease
Asp(D)-Pro(P) Weak acid, takes days
Asn(N)-Gly(G) Hydroxylamine
Hydrophobic Chymotrypsin, Pepsin, Thermolysin, Subtilisin, Papain
Created by: bek1826