Motifs and conformational analysis of amino acid residues adjoining β-turns in proteins

Ramakrishnan, C. ; Srinivasan, N. ; Nataraj, D. V. (1996) Motifs and conformational analysis of amino acid residues adjoining β-turns in proteins International Journal of Peptide and Protein Research, 48 (5). pp. 420-428. ISSN 0367-8377

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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1399-...

Related URL: http://dx.doi.org/10.1111/j.1399-3011.1996.tb00860.x

Abstract

Using a data set of 250 non-homologous high-resolution globular proteins, a systematic analysis of the conformations that precede and succeed (positions i and i+3) the various classical β-turn types has been carried out. The collective conformation of a specific β-turn type, including the flanking positions, termed motif, has been studied. In all the four turn types, the majority of examples are preceded and succeeded by extended conformation. Some of the other observations are: (1) In a type I β-turn, Gly at position i+3 has a higher favorability to occur with positive ø and does not prefer the major motif βαRR-β. (2) The left-handed alpha;-helical conformation (alpha;L) is not preferred at both the flanking positions for type I' and II β-turns, (3) The β-β motif is favourable for all the turn types and the motif β-αL very highly favourable for type I.

Item Type:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
Keywords:Analysis; β-turn; Conformation; Motifs
ID Code:41031
Deposited On:26 May 2011 07:00
Last Modified:27 May 2011 04:56

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