Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins

A Horovitz; A R Fersht

doi:10.1016/0022-2836(90)90275-Q

Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins

J Mol Biol. 1990 Aug 5;214(3):613-7. doi: 10.1016/0022-2836(90)90275-Q.

Authors

A Horovitz¹, A R Fersht

Affiliation

¹ Department of Chemistry, University of Cambridge, U.K.

PMID: 2388258
DOI: 10.1016/0022-2836(90)90275-Q

Abstract

Double mutant cycles enable the measurement of pairwise interactions in proteins. This method is extended for mutations at any number of positions in the protein. This provides a way for determining the context dependence of pairwise interactions on other neighbouring residues.

MeSH terms

Mutation*
Peptides / metabolism*
Protein Conformation
Proteins / metabolism*
Thermodynamics

Substances

Peptides
Proteins