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Article

Contribution of hydrophobic interactions to protein stability.

Journal of molecular biology - 6 May 2011

Pace C Nick, Fu Hailong, Fryar Katrina Lee, Landua John, Trevino Saul R, Shirley Bret A, Hendricks Marsha McNutt, Iimura Satoshi, Gajiwala Ketan, Scholtz J Martin, Grimsley Gerald R

Abstract excerpt

Our goal was to gain a better understanding of the contribution of hydrophobic interactions to protein stability. We measured the change in conformational stability, Δ(ΔG), for hydrophobic mutants of four proteins: villin headpiece subdomain (VHP) with 36 residues, a surface protein from Borrelia burgdorferi (VlsE) with 341 residues, and two proteins previously studied in our laboratory, ribonucleases Sa and T1....

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 21377472
DOI: 10.1016/j.jmb.2011.02.053
PMCID: PMC3086625

Provenance

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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