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During aging, in which the lenses are continuously exposed to ultraviolet irradiation and other environmental stresses, oxidation of tryptophan residues in \u03b2\/\u03b3\u2010crystallin is triggered and impacts the lens proteins to varying degrees. Kynurenine derivatives, formed by oxidation of tryptophan, accumulate, resulting in destabilization and insolubilization of \u03b2\/\u03b3\u2010crystallin, which correlates with age\u2010related cataract formation. To understand the contribution of tryptophan modification on the structure and stability of human \u03b2B2\u2010crystallin, five tryptophan residues were mutated to phenylalanine considering its similarity in structure and hydrophilicity to kynurenine. Among all mutants, W59F and W151F altered the stability and homo\u2010oligomerization of \u03b2B2\u2010crystallin\u2014W59F promoted tetramerization whereas W151F blocked oligomerization. Most W59F dimers transformed into tetramer in a month, and the separated dimer and tetramer of W59F demonstrated different structures and hydrophobicity, implying that the biochemical properties of \u03b2B2\u2010crystallin vary over time. By using SAXS, we found that the dimer of \u03b2B2\u2010crystallin in solution resembled the lattice \u03b2B1\u2010crystallin dimer (face\u2010en\u2010face), whereas the tetramer of \u03b2B2\u2010crystallin in solution resembled its lattice tetramer (domain\u2010swapped). Our results suggest that homo\u2010oligomerization of \u03b2B2\u2010crystallin includes potential inter\u2010subunit reactions, such as dissociation, unfolding, and re\u2010formation of the dimers into a tetramer in solution. The W&gt;F mutants are useful in studying different folding states of \u03b2B2\u2010crystallin in lens.<\/jats:p>","DOI":"10.1002\/pro.5092","type":"journal-article","created":{"date-parts":[[2024,6,26]],"date-time":"2024-06-26T16:57:41Z","timestamp":1719421061000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Characterization of <scp>\u03b2B2<\/scp>\u2010crystallin tryptophan mutants reveals two different folding states in solution"],"prefix":"10.1002","volume":"33","author":[{"given":"Jiayue","family":"Sun","sequence":"first","affiliation":[{"name":"Department of Chemistry, Graduate School of Science Kyoto University  Kyoto Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ken","family":"Morishima","sequence":"additional","affiliation":[{"name":"Institute for Integrated Radiation and Nuclear Science Kyoto University  Osaka 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