@inproceedings{00846299771e4013b4001167c129386f,
title = "Folding of β- and γ-peptides - the influence of substitution patterns on the formation of secondary structures",
abstract = "A symposium report. The protected and unprotected b2/b3-peptides form a helix with alternating 12- and 1-membered hydrogen-bonded rings in MeOH, i.e. the both peptides adopt the same conformation in soln. g2,3,4-Hexapeptide adopts a well defined (M)-2,614-helix in soln. The stability of this helix with increasing temp. was studied by 1D-1H NMR spectra in CD3OH. [on SciFinder (R)]",
keywords = "ACID, ACIDS, CONFORMATION, Chemical, Conformational Stability, FORM, NMR, PEPTIDE, PROTEIN, Peptides, Protein Folding, Proteins, SECONDARY STRUCTURE, SECONDARY-STRUCTURE, SPECTRA, STABILITY, Secondary, Structure, THERMAL-STABILITY, peptide folding secondary structure stability heli",
author = "Magnus Rueping and Bernhard Jaun and Dieter Seebach",
year = "2001",
language = "English (US)",
series = "Peptides: The Wave of the Future, Proceedings of the Second International and the Seventeenth American Peptide Symposium, San Diego, CA, United States, June 9-14, 2001",
booktitle = "Folding of β- and γ-peptides - the influence of substitution patterns on the formation of secondary structures",
}