Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.

doi:10.1074/jbc.M109.031344

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Article

Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.

The Journal of biological chemistry - 27 Nov 2009

Moreau Kate L, King Jonathan

Abstract excerpt

The human eye lens is composed of fiber cells packed with crystallins up to 450 mg/ml. Human gammaD-crystallin (HgammaD-Crys) is a monomeric, two-domain protein of the lens central nucleus. Both domains of this long lived protein have double Greek key beta-sheet folds with well packed hydrophobic...

Topics

Amino Acid Substitution
Animals
Binding Sites
Cataract
Circular Dichroism
Escherichia coli
Humans
Hydrophobic and Hydrophilic Interactions
Kinetics
Mice
Mutagenesis, Site-Directed
Mutant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Denaturation

Protein Folding

Protein Stability

Recombinant Proteins

Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 19758984
DOI: 10.1074/jbc.M109.031344
PMCID: PMC2785171

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-19758984-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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