Analysis of protein-protein interactions by mutagenesis: Direct versus indirect effects

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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 (Tyr42) 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.

Original languageEnglish
JournalProtein Engineering
Volume12
Issue1
Pages (from-to)41-45
Number of pages5
ISSN0269-2139
Publication statusPublished - 2 Feb 1999

    Research areas

  • Chymotrypsin inhibitor 2, Inhibitory activity, Loop flexibility, Protein-protein interactions, Stability, Subtilisin BPN'

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