Structural changes of α-crystallin during heating and comparisons with other small heat shock proteins

Regini, Justyn Wiktor ORCID: https://orcid.org/0000-0001-6149-5893 and Grossmann, J. Gunter 2003. Structural changes of α-crystallin during heating and comparisons with other small heat shock proteins. Fibre Diffraction Review 11 , pp. 95-101.

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Abstract

The small heat shock protein (sHSP) α-crystallin occurs in nearly all the major tissues of the body. It has two main functions; helping maintain transparency in the eye lens and as a molecular chaperone. We have investigated α-crystallin gels over a temperature range from 20 to 70oC using wide and low angle X-ray scattering techniques. The low angle data show a moderate increase in both the spacing and intensity of the reflection from 20 to 45oC. This was followed by a dramatic increase from 45 to 70oC. Upon cooling, this effect was found to be irreversible over an eleven-hour period. Wide-angle scattering reflections from the α- crystallin gel arise from the secondary structure organisation, and can be characterized by inter-sheet (a ring at ~10 Å) and intra-sheet (a ring at 4.7 Å) interactions which appear to respond differently to increasing temperature. However, no indications of denaturation or unfolding are noticeable throughout the temperature range.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Optometry and Vision Sciences
Subjects:	R Medicine > RE Ophthalmology
Uncontrolled Keywords:	Small heat shock protein (sHSP) ; α-crystallin ; Heating
ISSN:	1463-8401
Last Modified:	17 Oct 2022 09:40
URI:	https://orca.cardiff.ac.uk/id/eprint/5154

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