Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 6, Issue 19, Pages 4636-4641Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b407174c
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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=O stretching vibrations and in combination with force field and ab initio calculations it can unambiguously be derived that the peptide contains a stretched, beta-sheet related structure. Thus the peptide serves as an ideal candidate for beta-sheet model systems. By adding one water molecule to the peptide the beta-sheet related structure seems to be preserved with a water molecule being attached to the NHMe group.
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