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Conformational preferences of two peptides DYASL and DYA from haemagglutinin of influenza virus and their possible role in the initiation of protein folding

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Title Conformational preferences of two peptides DYASL and DYA from haemagglutinin of influenza virus and their possible role in the initiation of protein folding
 
Creator Prabha, C Raina
 
Description 325-331
The conformational preferences of two peptides
DYASL and DYA from haemagglutin in of influenza virus were studied using PClLO programme.
This was done to understand the possible role of DYAS in the initiation of
protein folding and to understand the contribution of the fourth residue serine
in the formation of turn . Our results indicate that this sequence shows an
inherent preference for turn conformation , with a stabilizing Asx turn . DYA
with NH group in the C-terminal protect ion models a type I β turn more closely
than DYAS, because serine has a weak potential for turn conformation.
 
Date 2012-12-08T16:12:16Z
2012-12-08T16:12:16Z
2002-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15209
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.39(5) [October 2002]