In:
Proteins: Structure, Function, and Bioinformatics, Wiley, Vol. 53, No. 2 ( 2003-11), p. 193-200
Abstract:
A genetic algorithm (GA)‐based strategy to dissect the determinants of peptide folding into α‐helix was developed. The structural information of helical peptides was obtained with respect to patterns of sequence variability. In many previously reported studies the intrinsic α‐helical propensities of amino acids although sequence‐dependent are apparently independent of the amino acid position. In this research, monomeric helical peptides selected from possible sequences produced by a GA‐chemical synthesis were analyzed to identify possible influential structural features. These hexadeca‐peptides were obtained after four successive generations. A total of 128 synthetic peptides were evaluated via circular dichroism (CD) measurements in aqueous solution, while the mean ellipticity at 222 nm confirmed the monomeric state of the peptides. The results presented here show that our GA‐based strategy may be useful in the design of proteins with increased α‐helix content. Proteins 2003. © 2003 Wiley‐Liss, Inc.
Type of Medium:
Online Resource
ISSN:
0887-3585
,
1097-0134
Language:
English
Publisher:
Wiley
Publication Date:
2003
detail.hit.zdb_id:
1475032-6
SSG:
12
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