Chain-length-dependent helical motifs and self-association of beta-peptides with constrained side chains

TitleChain-length-dependent helical motifs and self-association of beta-peptides with constrained side chains
Publication TypeJournal Article
AuthorsHetenyi, A, Mándity, IM, A. T, M, K. G, T, Fülöp, F
JournalJournal of the American Chemical Society
Volume127
Pagination547–RF, 2004, BIOCHEMISTRY-US, V43, P9527, DOI 10.1021/bi0494141
ISSN0002-7863
Abstract

Homo-oligomers constructed by using trans-2-aminocyclohexanecarboxylic acid monomers without protecting groups were studied. Both ab initio theory and NMR measurements showed that the tetramer tends to adopt a 10-helix motif, while the pentamer and hexamer form the known 14-helix. It was concluded that the conformationally constrained backbone is flexible enough to afford both 10-helical and 14-helical motifs, this observation in turn providing evidence of the true folding process. Self-association or the helical units was also detected, and the results of variable-temperature diffusion NMR measurements strongly suggested the presence of helical bundles in methanol solution.