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

被引:16
作者
Bloemendal, M
Toumadje, A
Johnson, WC
机构
[1] Free Univ Amsterdam, Dept Biophys, NL-1081 HV Amsterdam, Netherlands
[2] Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1999年 / 1432卷 / 02期
关键词
chaperone; CD spectroscopy; crystallin; alpha-helix; 3(10)-helix; secondary structure;
D O I
10.1016/S0167-4838(99)00107-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:234 / 238
页数:5
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