|Title||Chain-length-dependent helical motifs and self-association of beta-peptides with constrained side chains|
|Publication Type||Journal Article|
|Authors||Hetenyi, A, Mándity, IM, A. T, M, K. G, T, Fülöp, F|
|Journal||Journal of the American Chemical Society|
|Pagination||547–RF, 2004, BIOCHEMISTRY-US, V43, P9527, DOI 10.1021/bi0494141|
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.