{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T22:45:36Z","timestamp":1790203536898,"version":"4.1.0"},"reference-count":151,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2024,5,17]],"date-time":"2024-05-17T00:00:00Z","timestamp":1715904000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Science Foundation","award":["BMAT DMR-2002837"],"award-info":[{"award-number":["BMAT DMR-2002837"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Cataract disease is strongly associated with progressively accumulating oxidative damage to the extremely long-lived crystallin proteins of the lens. Cysteine oxidation affects crystallin folding, interactions, and light-scattering aggregation especially strongly due to the formation of disulfide bridges. Minimizing crystallin aggregation is crucial for lifelong lens transparency, so one might expect the ubiquitous lens crystallin superfamilies (\u03b1 and \u03b2\u03b3) to contain little cysteine. Yet, the Cys content of \u03b3-crystallins is well above the average for human proteins. We review literature relevant to this longstanding puzzle and take advantage of expanding genomic databases and improved machine learning tools for protein structure prediction to investigate it further. We observe remarkably low Cys conservation in the \u03b2\u03b3-crystallin superfamily; however, in \u03b3-crystallin, the spatial positioning of Cys residues is clearly fine-tuned by evolution. We propose that the requirements of long-term lens transparency and high lens optical power impose competing evolutionary pressures on lens \u03b2\u03b3-crystallins, leading to distinct adaptations: high Cys content in \u03b3-crystallins but low in \u03b2B-crystallins. Aquatic species need more powerful lenses than terrestrial ones, which explains the high methionine content of many fish \u03b3- (and even \u03b2-) crystallins. Finally, we discuss synergies between sulfur-containing and aromatic residues in crystallins and suggest future experimental directions.<\/jats:p>","DOI":"10.3390\/biom14050594","type":"journal-article","created":{"date-parts":[[2024,5,17]],"date-time":"2024-05-17T06:53:49Z","timestamp":1715928829000},"page":"594","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["The Functional Significance of High Cysteine Content in Eye Lens \u03b3-Crystallins"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1066-7143","authenticated-orcid":false,"given":"Eugene","family":"Serebryany","sequence":"first","affiliation":[{"name":"Department of Physiology & Biophysics, Stony Brook University, SUNY, Stony Brook, NY 11794, USA"},{"name":"Laufer Center for Physical & Quantitative Biology, Stony Brook University, SUNY, Stony Brook, NY 11794, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9996-7411","authenticated-orcid":false,"given":"Rachel W.","family":"Martin","sequence":"additional","affiliation":[{"name":"Department of Chemistry, UCI Irvine, Irvine, CA 92697-2025, USA"},{"name":"Department of Molecular Biology & Biochemistry, UCI Irvine, Irvine, CA 92697-3900, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1857-4363","authenticated-orcid":false,"given":"Gemma R.","family":"Takahashi","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology & Biochemistry, UCI Irvine, Irvine, CA 92697-3900, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,5,17]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1093\/oxfordjournals.molbev.a026406","article-title":"Relationship between the occurrence of cysteine in proteins and the complexity of organisms","volume":"17","author":"Miseta","year":"2000","journal-title":"Mol. 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