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Article

Crystal structural analysis of protein-protein interactions drastically destabilized by a single mutation.

Protein science : a publication of the Protein Society - 1 Jun 2008

Urakubo Yoshiaki, Ikura Teikichi, Ito Nobutoshi

Abstract excerpt

The complex of barnase (bn) and barstar (bs), which has been widely studied as a model for quantitative analysis of protein-protein interactions, is significantly destabilized by a single mutation, namely, bs Asp39 --> Ala, which corresponds to a change of 7.7 kcal x mol(-1) in the free energy of binding. However, there has been no structural information available to explain such a drastic destabilization. In the...

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Identifiers

PMID: 18441234
DOI: 10.1110/ps.073322508
PMCID: PMC2386745

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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