Modulation of the Structure and Stability of Novel Camel Lens Alpha-Crystallin by pH and Thermal Stress.

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

SUBMITTER: Malik A 

PROVIDER: S-EPMC9140948 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature