Table of Contents
International Journal of Proteomics
Volume 2014, Article ID 360230, 13 pages
Research Article

The Influence of Flanking Secondary Structures on Amino Acid Content and Typical Lengths of 3/10 Helices

1Department of General Chemistry, Belarusian State Medical University, Dzerzinskogo 83, 220116 Minsk, Belarus
2Laboratory of Cellular Technologies, Institute of Physiology, The National Academy of Sciences of Belarus, Academicheskaya 28, 220072 Minsk, Belarus

Received 15 July 2014; Revised 19 September 2014; Accepted 27 September 2014; Published 13 October 2014

Academic Editor: Thallapuranam K. Kumar

Copyright © 2014 Vladislav Victorovich Khrustalev et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

“PDBIDS” file includes PDB identifiers for proteins from each bacteria used in the main data set, as well as PDB indentifiers for nonbacterial proteins from the training set. “Ratios” file includes tables with ratios between amino acid usages in four types of connecting bridges (for “pure” random coil, for coil with 3/10 helices, for 3/10 helices 3 and 5 residues in length), as well as between amino acid usage in first five positions of alpha helices and in 3/10 helices 5 amino acid residues in length.

  1. Supplementary Materials