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Article

Protein stabilization and the Hofmeister effect: the role of hydrophobic solvation.

Biophysical journal - 4 Nov 2009

Tadeo Xavier, López-Méndez Blanca, Castaño David, Trigueros Tamara, Millet Oscar

Abstract excerpt

Using the IGg binding domain of protein L from Streptoccocal magnus (ProtL) as a case study, we investigated how the anions of the Hofmeister series affect protein stability. To that end, a suite of lysine-to-glutamine modifications were obtained and structurally and thermodynamically characterized. The changes in stability introduced with the mutation are related to the solvent-accessible area of the side chain,...

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Identifiers

PMID: 19883603
DOI: 10.1016/j.bpj.2009.08.029
PMCID: PMC2770621

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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