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

Hetényi, Anasztázia and Mándity, István and Martinek, Tamás and Tóth, Gábor and Fülöp, Ferenc (2005) Chain-length-dependent helical motifs and self-association of beta-peptides with constrained side chains. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 127 (2). pp. 547-553. ISSN 0002-7863

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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.

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