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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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Contributor : Jean-Luc Jestin Connect in order to contact the contributor
Submitted on : Thursday, November 21, 2013 - 5:22:19 PM
Last modification on : Thursday, April 7, 2022 - 10:10:30 AM
Long-term archiving on: : Saturday, February 22, 2014 - 4:42:33 AM


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  • HAL Id : pasteur-00907789, version 1



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



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