[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Raghavender, U.S. (2017) Analysis of residue conformations in peptides in Cambridge structural database and protein-peptide structural complexes. Chemical Biology & Drug Design, 89 (3). pp. 428-442. ISSN 17470277

[img] Text
Chem Biol Drug Design 89 p428.pdf
Restricted to Repository staff only

Download (2212Kb) | Request a copy

Abstract

A comprehensive statistical analysis of the geometric parameters of peptide chains in a reduced dataset of protein-peptide complexes in Protein Data Bank (PDB) is presented. The angular variables describing the backbone conformations of amino acid residues in peptide chains shed insights into the conformational preferences of peptide residues interacting with protein partners. Nonparametric statistical approaches are employed to evaluate the interrelationships and associations in structural variables. Grouping of residues based on their structure into chemical classes reveals characteristic trends in parameter relationships. A comparison of canonical amino acid residues in free peptide structures in Cambridge structural database (CSD) with identical residues in PDB complexes, suggests that the information can be integrated from both the structural repositories enabling efficient and accurate modeling of biologically active peptides.

Item Type: Article
Depositing User: Dr P Divakar
Date Deposited: 13 Apr 2017 10:19
Last Modified: 13 Apr 2017 10:21
URI: http://cdfd.sciencecentral.in/id/eprint/774

Actions (login required)

View Item View Item