Characterizing the topology of protein beta-sheets by an axis. - Institut Pasteur Access content directly
Other Publications Year : 2013

Characterizing the topology of protein beta-sheets by an axis.

Abstract

Beta-sheets and alpha-helices are the most frequent structural elements composing protein structures. Beta-sheets typically highlight complex curved and sequence-dependent surfaces of parallel and/or anti-parallel beta-strands. The topology of these curved surfaces are described in this work by a unique axis crossing all beta-sheet's strands. The distribution of the distances of the alpha carbons in each strand which are the closest to the axis is given. The frequency of the twenty amino acids along the axis is provided. Applications in the field of protein structure prediction are mentioned.
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Dates and versions

pasteur-00907789 , version 1 (21-11-2013)

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  • HAL Id : pasteur-00907789 , version 1

Cite

Jean-Luc Jestin, Bernard Caudron. Characterizing the topology of protein beta-sheets by an axis.. 2013. ⟨pasteur-00907789⟩

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