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Article

A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization.

Biophysical journal - 1 Nov 2005

Godoy-Ruiz Raquel, Perez-Jimenez Raul, Ibarra-Molero Beatriz, Sanchez-Ruiz Jose M

Abstract excerpt

We have determined the effect of mutations involving isoleucine and valine (i.e., mutations I-->V and V-->I) on the stability of Escherichia coli thioredoxin. Despite the similarity in chemical structure (V and I differ only in a methyl group), we find that many environments are optimized to a significant extent for either V or I. We find, furthermore, that a plot of effect of hydrophobic mutations on stability...

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Identifiers

PMID: 16100262
DOI: 10.1529/biophysj.105.067025
PMCID: PMC1366828

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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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