Daura, XavierGademann, KarlJaun, BernhardSeebach, DieterVanGunsteren, Wilfred F.Mark, Alan E.2006-11-222006-11-22199910.1002/(SICI)1521-3773(19990115)38:1/2<236::AID-ANIE236>3.0.CO;2-Mhttps://infoscience.epfl.ch/handle/20.500.14299/235810Mol. dynamics simulation studies on the folding of beta-peptides H-beta3-HVal-beta3-HAla-beta3-HLeu-(S,S)-beta3-HAla(alphaMe)-beta3-HVal-beta3-HAla-beta3-HLeu-OH and H-beta2-HVal-beta3-HAla-beta2-HLeu-beta3-HVal-beta2-HAla-beta3-HLeu-OH were carried out. Despite the small differences in sequence between the two peptides studied, the simulations correctly predict a left-handed 31-helical fold for the beta-heptapeptide and a right-handed helical fold for the beta-hexapeptide.simulation folding beta peptidetext::journal::journal article::research article