<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Malik A</submitter><funding>King Saud University</funding><pagination>273</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9140948</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(5)</volume><pubmed_abstract>Alpha-crystallin protein performs structural and chaperone functions in the lens and comprises alphaA and alphaB subunits at a molar ratio of 3:1. The highly complex alpha-crystallin structure challenges structural biologists because of its large dynamic quaternary structure (300-1000 kDa). Camel lens alpha-crystallin is a poorly characterized molecular chaperone, and the alphaB subunit possesses a novel extension at the N-terminal domain. We purified camel lens alpha-crystallin using size exclusion chromatography, and the purity was analyzed by gradient (4-12%) sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Alpha-crystallin was equilibrated in the pH range of 1.0 to 7.5. Subsequently, thermal stress (20-94 °C) was applied to the alpha-crystallin samples, and changes in the con</pubmed_abstract><journal>Gels (Basel, Switzerland)</journal><pubmed_title>Modulation of the Structure and Stability of Novel Camel Lens Alpha-Crystallin by pH and Thermal Stress.</pubmed_title><pmcid>PMC9140948</pmcid><funding_grant_id>RSP-2021/360</funding_grant_id><pubmed_authors>Malik A</pubmed_authors><pubmed_authors>Alhomida AS</pubmed_authors><pubmed_authors>Khan JM</pubmed_authors><pubmed_authors>Ola MS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Modulation of the Structure and Stability of Novel Camel Lens Alpha-Crystallin by pH and Thermal Stress.</name><description>Alpha-crystallin protein performs structural and chaperone functions in the lens and comprises alphaA and alphaB subunits at a molar ratio of 3:1. The highly complex alpha-crystallin structure challenges structural biologists because of its large dynamic quaternary structure (300-1000 kDa). Camel lens alpha-crystallin is a poorly characterized molecular chaperone, and the alphaB subunit possesses a novel extension at the N-terminal domain. We purified camel lens alpha-crystallin using size exclusion chromatography, and the purity was analyzed by gradient (4-12%) sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Alpha-crystallin was equilibrated in the pH range of 1.0 to 7.5. Subsequently, thermal stress (20-94 °C) was applied to the alpha-crystallin samples, and changes in the con</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Apr</publication><modification>2025-04-04T10:42:38.377Z</modification><creation>2025-04-04T10:42:38.377Z</creation></dates><accession>S-EPMC9140948</accession><cross_references><pubmed>35621572</pubmed><doi>10.3390/gels8050273</doi></cross_references></HashMap>