Document Detail

Prediction and Fourier-transform infrared-spectroscopy estimation of the secondary structure of a recombinant beta-glucosidase from Streptomyces sp. (ATCC 11238).
MedLine Citation:
PMID:  8948434     Owner:  NLM     Status:  MEDLINE    
The secondary structure of a recombinant beta-glucosidase (EC from Streptomyces sp. (ATCC 11238) has been predicted by computer algorithms and also estimated by Fourier-transform IR spectroscopy. From curve fitting of the deconvoluted IR spectra, the most probable distribution of the secondary-structural classes appears to be about 34% alpha-helix, 30% beta-sheet, 25% reverse turns and 11% non-ordered structures. These data showed a good agreement with data from computer prediction (35% alpha-helix, 23% beta-sheet, 31% reverse turns and 11% non-ordered structures).
J A Perez-Pons; E Padros; E Querol
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  308 ( Pt 3)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1995 Jun 
Date Detail:
Created Date:  1997-01-07     Completed Date:  1997-01-07     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  791-4     Citation Subset:  IM    
Institut de Biologica Fonamental, Universitat Autònoma de Barcelona, Spain.
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MeSH Terms
Amino Acid Sequence
Binding Sites
Molecular Sequence Data
Protein Structure, Secondary*
Recombinant Proteins / chemistry,  genetics
Sequence Alignment
Spectroscopy, Fourier Transform Infrared
Streptomyces / enzymology*
beta-Glucosidase / chemistry*
Reg. No./Substance:
0/Recombinant Proteins; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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