Seebach, DieterGademann, KarlSchreiber, Jurg V.Matthews, Jennifer L.Hintermann, TobiasJaun, BernhardOberer, LukasHommel, UlrichWidmer, Hans2006-11-222006-11-22199710.1002/hlca.19970800703https://infoscience.epfl.ch/handle/20.500.14299/235806beta-Hexapeptides and a beta-dodecapeptide with sequences contg. two different types of beta-amino acids, aliph. proteinaceous side-chains in 2- or 3-position, were studied with CD and NMR measurements. With one exception, the secondary structures formed by these beta-peptides differ from those of isomers studied previously. Detailed NMR anal. of the beta-hexapeptide with alternating beta2,beta3-building blocks, and mol.-dynamics simulations revealed a min. energy conformation which is described as a novel irregular helix contg. 10- and 12-membered H-bonded rings.β peptide helicalsecondary structureconformationhelical conformationtext::journal::journal article::research article