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Article

Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin.

Protein science : a publication of the Protein Society - 1 Mar 2005

Flaugh Shannon L, Kosinski-Collins Melissa S, King Jonathan

Abstract excerpt

Human gammaD-crystallin (HgammaD-Crys) is a monomeric eye lens protein composed of two highly homologous beta-sheet domains. The domains interact through interdomain side chain contacts forming two structurally distinct regions, a central hydrophobic cluster and peripheral residues. The hydrophobic cluster contains Met43, Phe56, and Ile81 from the N-terminal domain (N-td) and Val132, Leu145, and Val170 from the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 15722442
DOI: 10.1110/ps.041111405
PMCID: PMC2279286

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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