학술논문
Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects
Document Type
Article
Author
Source
Protein Engineering Design and Selection; January 1999, Vol. 12 Issue: 1 p41-45, 5p
Subject
Language
ISSN
17410126; 17410134
Abstract
Site-directed mutagenesis, including double-mutant cycles, is used routinely for studying protein-protein interactions. We now present a case analysis of chymotrypsin inhibitor 2 (CI2) and subtilisin BPN' using (i) a residue in CI2 that is known to interact directly with subtilisin (Tyr142) and (ii) two CI2 residues that do not have direct contacts with subtilisin (Arg46 and Arg48). We find that there are similar changes in binding energy on mutation of these two sets of residues. It can thus be difficult to interpret mutagenesis data in the absence of structural information.Keywords: chymotrypsin inhibitor 2/inhibitory activity/loop flexibility/protein-protein interactions/stability/subtilisin BPN'