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In this study, cataract\u2010causing familial mutations, P20R and A171T, were introduced in <jats:italic>CRY\u0410B<\/jats:italic> gene. After successful expression in <jats:styled-content style=\"fixed-case\"><jats:italic>Escherichia coli<\/jats:italic><\/jats:styled-content> and subsequent purification, the recombinant proteins were subjected to extensive structural and functional analyses using various spectroscopic techniques, gel electrophoresis, and electron microscopy. The results of fluorescence and Raman assessments suggest important but discreet conformational changes in human \u03b1B\u2010Cry upon these cataractogenic mutations. Furthermore, the mutant proteins exhibited significant secondary structural alteration as revealed by FTIR and Raman spectroscopy. An increase in conformational stability was seen in the human \u03b1B\u2010Cry bearing these congenital cataractogenic mutations. The oligomeric size distribution and chaperone\u2010like activity of human \u03b1B\u2010Cry were significantly altered by these mutations. The P20R mutant protein was observed to loose most of the chaperone\u2010like activity. Finally, these cataractogenic mutant proteins exhibited an increased propensity to form the amyloid fibrils when incubated under environmental stress. Overall, the structural and functional changes in mutated human \u03b1B\u2010Cry proteins can shed light on the pathogenic development of congenital cataracts.<\/jats:p>","DOI":"10.1002\/bip.23350","type":"journal-article","created":{"date-parts":[[2020,2,28]],"date-time":"2020-02-28T16:24:12Z","timestamp":1582907052000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["The congenital cataract\u2010causing mutations P20R and A171T are associated with important changes in the amyloidogenic feature, structure and chaperone\u2010like activity of human \u03b1B\u2010crystallin"],"prefix":"10.1002","volume":"111","author":[{"given":"Maryam","family":"Ghahramani","sequence":"first","affiliation":[{"name":"Protein Chemistry Laboratory (PCL), Department of Biology College of Sciences, Shiraz University  Shiraz Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7396-7720","authenticated-orcid":false,"given":"Reza","family":"Yousefi","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory (PCL), Department of Biology College of Sciences, Shiraz University  Shiraz Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ali","family":"Niazi","sequence":"additional","affiliation":[{"name":"Institute of Biotechnology Shiraz University  Shiraz Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Boris","family":"Kurganov","sequence":"additional","affiliation":[{"name":"Bach Institute of Biochemistry Research Center of Biotechnology of the Russian Academy of Sciences  Moscow Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2020,2,28]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.pbiomolbio.2003.11.012"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biocel.2012.02.015"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.21.10449"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-4835(02)00278-6"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/eye.1999.114"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1080\/02713683.2017.1324628"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbagen.2015.03.012"},{"key":"e_1_2_8_9_1","first-page":"2936","volume":"33","author":"Gopalakrishnan S.","year":"1992","journal-title":"Investig. 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