alexa Applications of model beta-hairpin peptides.
Bioinformatics & Systems Biology

Bioinformatics & Systems Biology

Journal of Proteomics & Bioinformatics

Author(s): Stotz CE, Topp EM

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Abstract In recent years, beta-hairpin peptides have been studied in great detail. Much of the focus has been on the thermodynamic stability of beta-hairpin structure. Structural measurements have been conducted with nuclear magnetic resonance, with additional information obtained from circular dichroism, Fourier transform infrared, and molecular dynamic simulation studies. Point mutations, both in the beta-strands and in the turn region, have systematically explored the role of turn sequence, side-chain-side-chain interactions, intramolecular hydrogen bonding, and beta-strand length on beta-hairpin peptide conformational stability. In addition to studying the elements of structural stability independently, the cooperative nature of the individual components to combine to form the overall structure has also been investigated. Because the beta-hairpin peptides often spontaneously form their conformation, they have begun to serve as models for studying peptide binding and therapeutic agents. (c) 2004 Wiley-Liss, Inc. and the American Pharmacists Association This article was published in J Pharm Sci and referenced in Journal of Proteomics & Bioinformatics

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