@inproceedings{49e86f2409964521b6fb3058b5ac16d0,
title = "Synthesis and structural investigations of a a-hydroxylated b-hexapeptide",
abstract = "(2S,3S)-a-Hydroxy-b3-Hleu, -b3-HAla and -b3-HVal-amino acids were prepd. and used for the synthesis of a b-hexapeptide. The resulting a-hydroxylated-b3-hexapeptide (terminally protected) and its fully deprotected form are insol. in most org. solvents including MeOH and fluorinated alcs., suggesting that they form aggregates or that they adopt a sheet-like conformation. Their phys. properties prevented any CD spectroscopic investigations and limited the possibilities of NMR spectroscopy. [on SciFinder (R)]",
keywords = "ACID, ACIDS, CONFORMATION, Chemical, FORM, NMR, NMR Spectroscopy, NMR-SPECTROSCOPY, PEPTIDE, PROTEIN, Peptides, Proteins, SPECTROSCOPY, Solvents, Structural, Synthesis, beta hexapeptide alpha hydroxy beta amino acid syn",
author = "Francois Gessier and Magnus Rueping and Dieter Seebach",
year = "2002",
language = "English (US)",
series = "Peptides 2002, Proceedings of the European Peptide Symposium, 27th, Sorrento, Italy, Aug.31-Sept.6, 2002",
booktitle = "Synthesis and structural investigations of a a-hydroxylated b-hexapeptide",
}