Gademann, KarlHane, AndreasRueping, MagnusJaun, BernhardSeebach, Dieter2006-11-222006-11-22200310.1002/anie.200250290https://infoscience.epfl.ch/handle/20.500.14299/235832The authors report compelling evidence for the formation of a fourth type of helical secondary structure of a beta-peptide in MeOH, and this phenomenon occurs if each amino acid has a hydroxy group in the 2-position. 2D-NMR expts. of terminally-protected beta-hexapeptide I were conducted to obtain its secondary structure information.amino acidsβ-peptidesconformational analysispeptidomimeticssecondary structureThe fourth helical secondary structure of β-peptides: The (P)-28-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residuestext::journal::journal article::research article