Bovine lens crystallins do contain helical structure: a circular dichroism study

In order to settle a recent discussion on the secondary structure of lens crystallins, we have measured the circular dichroism (CD) spectra of α-, β H-, and β L-crystallin from 178 to 250 nm and of γ-crystallin from 168 to 250 nm. The results were analysed by means of a newly developed algorithm tha...

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Bibliographic Details
Published in:Biochimica et biophysica acta 1999-07, Vol.1432 (2), p.234-238
Main Authors: Bloemendal, Michael, Toumadje, Arazdordi, Johnson, W.Curtis
Format: Article
Language:English
Subjects:
3 10-helix
Animals
Cattle
CD spectroscopy
Chaperone
Circular Dichroism
Crystallin
Crystallins - chemistry
Crystallins - genetics
Protein Structure, Secondary
Secondary structure
Software
α-helix
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Summary:In order to settle a recent discussion on the secondary structure of lens crystallins, we have measured the circular dichroism (CD) spectra of α-, β H-, and β L-crystallin from 178 to 250 nm and of γ-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 α- and 3 10-helical, and between extended and polyproline β-type structure. The results indicate that the crystallins studied contain a non-negligible amount of α-helical structure, although at least 50% of it is in the form of single and/or distorted loops. In α-crystallin, which is related to the chaperones, the helical content is lower than in β- and γ-crystallin. In some cases, the helices may play a role in DNA binding by the crystallins.
ISSN:0167-4838
0006-3002
1879-2588
DOI:10.1016/S0167-4838(99)00107-7