Document Detail

A predicted secondary structure of protein protease inhibitors.
MedLine Citation:
PMID:  7342589     Owner:  NLM     Status:  MEDLINE    
Basing on the Chou & Fasman method (Biochemistry, 13, 222-245; 1974) and the known amino acid sequences, the alpha-helical, beta-sheet, beta-turn and random-coil regions were predicted for protein protease inhibitors. It appears that in all the inhibitors examined there is a region conserved in the vicinity of the active site, composed of one beta-turn with an adjacent beta-sheet structure, and a second beta-turn situated in the other part of the polypeptide chain and linked with the first one by disulphide bridge. Two disulphide bridges between Cys2 and Cys25, and between Cys10 and Cys21 were proposed for the squash seed inhibitor. It is suggested that the two beta-turns play an essential role in the process of trypsin inhibition by protein protease inhibitors.
P Tłomak; K Nowak
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Acta biochimica Polonica     Volume:  28     ISSN:  0001-527X     ISO Abbreviation:  Acta Biochim. Pol.     Publication Date:  1981  
Date Detail:
Created Date:  1982-07-19     Completed Date:  1982-07-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  14520300R     Medline TA:  Acta Biochim Pol     Country:  POLAND    
Other Details:
Languages:  eng     Pagination:  241-51     Citation Subset:  IM    
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MeSH Terms
Amino Acid Sequence
Protease Inhibitors*
Protein Conformation*
Trypsin Inhibitor, Kunitz Soybean
Reg. No./Substance:
0/Protease Inhibitors; 9088-41-9/Trypsin Inhibitor, Kunitz Soybean

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