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Elucidating the folding problem of helical peptides using empirical parameters

Nature Structural Biology volume 1, pages 399–409 (1994)Cite this article

Abstract

Using an empirical analysis of experimental data we have estimated a set of energy contributions which accounts for the stability of isolated α-helices. With this database and an algorithm based on statistical mechanics, we describe the average helical behaviour in solution of 323 peptides and the helicity per residue of those peptides analyzed by nuclear magnetic resonance. Moreover the algorithm successfully detects the α-helical tendency, in solution, of a peptide corresponding to a β-strand of ubiquitin.

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Muñoz, V., Serrano, L. Elucidating the folding problem of helical peptides using empirical parameters. Nat Struct Mol Biol 1, 399–409 (1994). https://doi.org/10.1038/nsb0694-399

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