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

Abstract

<span style="font-size:14.0pt;font-family:" times="" new="" roman";="" mso-fareast-font-family:"times="" roman";mso-ansi-language:en-us;mso-fareast-language:="" en-us;mso-bidi-language:ar-sa"="">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.</span>