Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Prediction of peptide structure: How far are we?

Prediction of peptide structure: How far are we? Rational design of peptides is a challenge, which would benefit from a better knowledge of the rules of sequence–structure–function relationships. Peptide structures can be approached by spectroscopy and NMR techniques but data from these approaches too frequently diverge. Structures can also be calculated in silico from primary sequence information using three algorithms: Pepstr, Robetta, and PepLook. The most recent algorithm, PepLook introduces indexes for evaluating structural polymorphism and stability. For peptides with converging experimental data, calculated structures from PepLook and, to a lesser extent from Pepstr, are close to NMR models. The PepLook index for polymorphism is low and the index for stability points out possible binding sites. For peptides with divergent experimental data, calculated and NMR structures can be similar or, can be different. These differences are apparently due to polymorphism and to different conditions of structure assays and calculations. The PepLook index for polymorphism maps the fragments encoding disorder. This should provide new means for the rational design of peptides. Proteins 2006. © 2006 Wiley‐Liss, Inc. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Proteins: Structure Function and Bioinformatics Wiley

Prediction of peptide structure: How far are we?

Download PDF
9 pages

Loading next page...
 
/lp/wiley/prediction-of-peptide-structure-how-far-are-we-m9V8D0bAYX

References (43)

Publisher
Wiley
Copyright
Copyright © 2006 Wiley Subscription Services
ISSN
0887-3585
eISSN
1097-0134
DOI
10.1002/prot.21151
pmid
17019719
Publisher site
See Article on Publisher Site

Abstract

Rational design of peptides is a challenge, which would benefit from a better knowledge of the rules of sequence–structure–function relationships. Peptide structures can be approached by spectroscopy and NMR techniques but data from these approaches too frequently diverge. Structures can also be calculated in silico from primary sequence information using three algorithms: Pepstr, Robetta, and PepLook. The most recent algorithm, PepLook introduces indexes for evaluating structural polymorphism and stability. For peptides with converging experimental data, calculated structures from PepLook and, to a lesser extent from Pepstr, are close to NMR models. The PepLook index for polymorphism is low and the index for stability points out possible binding sites. For peptides with divergent experimental data, calculated and NMR structures can be similar or, can be different. These differences are apparently due to polymorphism and to different conditions of structure assays and calculations. The PepLook index for polymorphism maps the fragments encoding disorder. This should provide new means for the rational design of peptides. Proteins 2006. © 2006 Wiley‐Liss, Inc.

Journal

Proteins: Structure Function and Bioinformatics – Wiley

Published: Jan 1, 2006

Keywords: ; ; ; ; ;

There are no references for this article.