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Article

Characterization of βB2-crystallin tryptophan mutants reveals two different folding states in solution.

Protein science : a publication of the Protein Society - 1 Jul 2024

Sun Jiayue, Morishima Ken, Inoue Rintaro, Sugiyama Masaaki, Takata Takumi

Abstract excerpt

Conserved tryptophan residues are critical for the structure and the stability of β/γ-crystallin in the lenses of vertebrates. During aging, in which the lenses are continuously exposed to ultraviolet irradiation and other environmental stresses, oxidation of tryptophan residues in β/γ-crystallin is triggered and impacts the lens proteins to varying degrees. Kynurenine derivatives, formed by oxidation of...

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Identifiers

PMID: 38924206
DOI: 10.1002/pro.5092
PMCID: PMC11201810

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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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