Issue 19, 2004

Structure of the tripeptide model Ac–Val–Tyr(Me)–NHMe and its cluster with water investigated by IR/UV double resonance spectroscopy

Abstract

In this paper the structures of the isolated tripeptide model Ac–Val–Tyr(Me)–NHMe (Val = valine, Tyr = tyrosine) and its cluster with water are investigated by mass-, isomer- and state-selective IR/UV double resonance spectroscopy. From the IR spectra both in the region of the NH and C[double bond, length as m-dash]O stretching vibrations and in combination with force field and ab initio calculations it can unambiguously be derived that the peptide contains a stretched, β-sheet related structure. Thus the peptide serves as an ideal candidate for β-sheet model systems. By adding one water molecule to the peptide the β-sheet related structure seems to be preserved with a water molecule being attached to the NHMe group.

Article information

Article type
Paper
Submitted
12 May 2004
Accepted
07 Sep 2004
First published
16 Sep 2004

Phys. Chem. Chem. Phys., 2004,6, 4636-4641

Structure of the tripeptide model Ac–Val–Tyr(Me)–NHMe and its cluster with water investigated by IR/UV double resonance spectroscopy

H. Fricke, A. Gerlach, C. Unterberg, P. Rzepecki, T. Schrader and M. Gerhards, Phys. Chem. Chem. Phys., 2004, 6, 4636 DOI: 10.1039/B407174C

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