Issue 32, 2007
From the journal:

Physical Chemistry Chemical Physics

Secondary structure binding motifs of the jet cooled tetrapeptide model Ac–Leu–Val–Tyr(Me)–NHMe

H. Fricke,a   G. Schäfer,b   T. Schraderc  and  M. Gerhards*a  

* Corresponding authors

a Heinrich-Heine Universität Düsseldorf, Institut für Physikalische Chemie I, Universitätsstraße 26.33.O2, 40225 Düsseldorf, and TU Kaiserslautern, Fachbereich Chemie, Erwin-Schrödingerstr. 52, Kaiserslautern, Germany
E-mail: gerhards@chemie.uni-kl.de

b Fachbereich Chemie, Philipps-Universität Marburg, Hans-Meerwein-Str., Marburg, Germany

c Universität Duisburg-Essen, Fachbereich Chemie, Institut für Organische Chemie, Universitätsstrasse 5, Essen, Germany

Abstract

In this paper the structure of the isolated tetrapeptide model Ac–Leu–Val–Tyr(Me)–NHMe (Leu = leucine, Val = valine, Tyr = tyrosine) is investigated by mass- and isomer-selective IR/UV double resonance spectroscopy. Two isomers of this peptide are observed and in combination with force field, ab initio, and DFT calculations these structures are assigned to folded arrangements presenting two different secondary structure binding motifs: (a) a combined γ-turn/β-turn structure and (b) a triple γ-turn structure, which is described for the first time for an isolated model system in the gas phase.

Graphical abstract: Secondary structure binding motifs of the jet cooled tetrapeptide model Ac–Leu–Val–Tyr(Me)–NHMe

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Article information

DOI
https://doi.org/10.1039/B706519A
Article type
Paper
Submitted
30 Apr 2007
Accepted
11 Jul 2007
First published
25 Jul 2007

Phys. Chem. Chem. Phys., 2007,9, 4592-4597

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Secondary structure binding motifs of the jet cooled tetrapeptide model Ac–Leu–Val–Tyr(Me)–NHMe

H. Fricke, G. Schäfer, T. Schrader and M. Gerhards, Phys. Chem. Chem. Phys., 2007, 9, 4592 DOI: 10.1039/B706519A

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