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Article

Destabilizing mutations alter the hydrogen exchange mechanism in ribonuclease A.

Biophysical journal - 15 Mar 2008

Bruix Marta, Ribó Marc, Benito Antoni, Laurents Douglas V, Rico Manuel, Vilanova Maria

Abstract excerpt

The effect of strongly destabilizing mutations, I106A and V108G of Ribonuclease A (RNase A), on its structure and stability has been determined by NMR. The solution structures of these variants are essentially equivalent to RNase A. The exchange rates of the most protected amide protons in RNase A (35 degrees C), the I106A variant (35 degrees C), and the V108G variant (10 degrees C) yield stability values of 9.9,...

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Identifiers

PMID: 18192347
DOI: 10.1529/biophysj.107.122952
PMCID: PMC2257908

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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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