Issue 7, 2001
From the journal:

Chemical Communications

Design, machine synthesis, and NMR-solution structure of a β-heptapeptide forming a salt-bridge stabilised 314-helix in methanol and in waterElectronic supplementary information (ESI) available: NMR spectroscopy and conc. dependent CD-spectra of 1. See http://www.rsc.org/suppdata/cc/b1/b101085i/

Per I. Arvidsson,a   Magnus Ruepinga  and  Dieter Seebach*a  

* Corresponding authors

a Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule, ETH-Zentrum, Universitätstrasse 16, Zürich, Switzerland.
E-mail: seebach@org.chem.ethz.ch

Abstract

Salt-bridge formation may be used to stabilise the 314-helical conformation of β-peptides in aqueous solution, as shown by a 2D-NMR spectroscopic investigation.

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Article information

DOI
https://doi.org/10.1039/B101085I
Article type
Communication
Submitted
31 Jan 2001
Accepted
28 Feb 2001
First published
12 Mar 2001

Chem. Commun., 2001, 649-650

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Design, machine synthesis, and NMR-solution structure of a β-heptapeptide forming a salt-bridge stabilised 314-helix in methanol and in water

P. I. Arvidsson, M. Rueping and D. Seebach, Chem. Commun., 2001, 649 DOI: 10.1039/B101085I

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