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

article complémentaire de : Guilloux A, Caudron B, Jestin JL (2013) A method to predict edge strands in beta-sheets from protein sequences. Computational and Structural Biotechnology Journal. 7 (9): e201305001. doi: http://dx.doi.org/10.5936/csbj.201305001Beta-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