{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Malik A"],"funding":["King Saud University"],"pagination":["273"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9140948"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(5)"],"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"],"journal":["Gels (Basel, Switzerland)"],"pubmed_title":["Modulation of the Structure and Stability of Novel Camel Lens Alpha-Crystallin by pH and Thermal Stress."],"pmcid":["PMC9140948"],"funding_grant_id":["RSP-2021/360"],"pubmed_authors":["Malik A","Alhomida AS","Khan JM","Ola MS"],"additional_accession":[]},"is_claimable":false,"name":"Modulation of the Structure and Stability of Novel Camel Lens Alpha-Crystallin by pH and Thermal Stress.","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","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2025-04-04T10:42:38.377Z","creation":"2025-04-04T10:42:38.377Z"},"accession":"S-EPMC9140948","cross_references":{"pubmed":["35621572"],"doi":["10.3390/gels8050273"]}}