Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins
A Horovitz, AR Fersht - Journal of molecular biology, 1990 - Elsevier
A Horovitz, AR Fersht
Journal of molecular biology, 1990•ElsevierDouble 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.
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.
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.
Elsevier