Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity.

doi:10.1021/bi00250a042

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Article

Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity.

Biochemistry - 22 Nov 1994

Jackson S E, Fersht A R

Abstract excerpt

Residues in the active site loop of the serine protease inhibitor, chymotrypsin inhibitor 2, thought to play an important role in loop stability and inhibitory activity, have been investigated by site-directed mutagenesis. Substitutions at residues 58 (threonine in wild type) and 60 (glutamic acid in wild type), which flank the scissile bond (Met-59-Glu-60) and are conserved among the potato inhibitor I family of...

Topics

Amino Acid Sequence
Aspartic Acid
Binding Sites
Chymotrypsin
Glutamic Acid
Kinetics
Molecular Sequence Data
Mutation
Peptides
Plant Proteins
Protein Denaturation
Protein Structure, Secondary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Structure, Tertiary

Sequence Homology, Amino Acid

Solanum tuberosum

Subtilisins

Thermodynamics

Threonine

Source

Open in PubMed

Identifiers

PMID: 7947796
DOI: 10.1021/bi00250a042

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7947796-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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