Biochemistry
Which amino acid residues does trypsin specifically cleave peptide bonds after?
A peptide sequence contains a proline residue. How does this affect the cleavage by peptidases?
How does the specificity of trypsin differ from chymotrypsin?
Which residues does chymotrypsin slowly cleave over time, apart from its preferred aromatic residues?
Which amino acid residues are excluded from elastase's cleavage specificity?
Thrombin cleaves peptide bonds specifically after which amino acid residue?
In a peptide sequence, the presence of proline affects peptidase activity by:
