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- W2018731421 abstract "The small heat shock protein (sHSP) I±-crystallin occurs in nearly all the major tissues of the body. It has twomain functions; helping maintain transparency in the eye lens and as a molecular chaperone. We haveinvestigated I±-crystallin gels over a temperature range from 20 to 70oC using wide and low angle X-rayscattering techniques. The low angle data show a moderate increase in both the spacing and intensity of thereflection from 20 to 45oC. This was followed by a dramatic increase from 45 to 70oC. Upon cooling, thiseffect was found to be irreversible over an eleven-hour period. Wide-angle scattering reflections from the I±-crystallin gel arise from the secondary structure organisation, and can be characterized by inter-sheet (a ringat ~10 A…) and intra-sheet (a ring at 4.7 A…) interactions which appear to respond differently to increasingtemperature. However, no indications of denaturation or unfolding are noticeable throughout thetemperature range." @default.
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- W2018731421 date "2003-01-01" @default.
- W2018731421 modified "2023-09-25" @default.
- W2018731421 title "Structural changes of α-crystallin during heating and comparisons with other small heat shock proteins" @default.
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- W2018731421 doi "https://doi.org/10.1382/s20031195" @default.
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