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• W1968132007 abstract "In order to settle a recent discussion on the secondary structure of lens crystallins, we have measured the circular dichroism (CD) spectra of alpha-, beta(H)-, and beta(L)-crystallin from 178 to 250 nm and of gamma-crystallin from 168 to 250 nm. The results were analysed by means of a newly developed algorithm that almost doubles the reliability of secondary structure prediction and that allows discrimination between alpha- and 3(10)-helical, and between extended and polyproline beta-type structure. The results indicate that the crystallins studied contain a non-negligible amount of alpha-helical structure, although at least 50% of it is in the form of single and/or distorted loops. In alpha-crystallin, which is related to the chaperones, the helical content is lower than in beta- and gamma-crystallin. In some cases, the helices may play a role in DNA binding by the crystallins." @default.
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• W1968132007 date "1999-07-01" @default.
• W1968132007 modified "2023-09-23" @default.
• W1968132007 title "Bovine lens crystallins do contain helical structure: a circular dichroism study" @default.
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• W1968132007 doi "https://doi.org/10.1016/s0167-4838(99)00107-7" @default.
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