Document Detail

Bovine lens crystallins do contain helical structure: a circular dichroism study.
MedLine Citation:
PMID:  10407145     Owner:  NLM     Status:  MEDLINE    
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.
M Bloemendal; A Toumadje; W C Johnson
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1432     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1999 Jul 
Date Detail:
Created Date:  1999-08-20     Completed Date:  1999-08-20     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  234-8     Citation Subset:  IM    
Department of Biophysics, Free University, De Boelelaan 1081, 1081 HV, Amsterdam, Netherlands.
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MeSH Terms
Circular Dichroism
Crystallins / chemistry*,  genetics
Protein Structure, Secondary
Reg. No./Substance:

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