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Exploration of structural features of monomeric helical peptides designed with a genetic algorithm
Author(s) -
Zhang Wuming,
Loughran Micheal G.,
Kanna Shinichi,
Yano Kazuyoshi,
Ikebukuro Kazunori,
Yokobayashi Yohei,
Kuroda Reiko,
Karube Isao
Publication year - 2003
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10509
Subject(s) - monomer , circular dichroism , sequence (biology) , peptide , amino acid , helix (gastropod) , peptide sequence , chemistry , protein folding , folding (dsp implementation) , crystallography , biochemistry , biology , polymer , gene , ecology , organic chemistry , snail , electrical engineering , engineering
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.