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pubmed-article:18345665pubmed:abstractTextAn isolated beta-sheet model system is investigated in a molecular beam experiment by means of mass- and isomer-selective IR/R2PI double resonance spectroscopy as well as ab initio and DFT calculations. As the exclusive intermolecular assembly, a beta-sheet motif is formed by spontaneous dimerization of two isolated peptide molecules. This secondary structure is produced from the tripeptide model Ac-Val-Tyr(Me)-NHMe without any further environment to form the binding motif which is analyzed by both the characteristic amide A and I vibrations. The experimental and theoretical investigations yield the assignment to an antiparallel beta-sheet model. The result of this detailed spectroscopic analysis on an isolated beta-sheet model indicates that there are intrinsic properties of a beta-sheet structure which can be formed without a solvent or a peptidic environment.lld:pubmed
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pubmed-article:18345665pubmed:year2008lld:pubmed
pubmed-article:18345665pubmed:articleTitleInvestigation of secondary structure elements by IR/UV double resonance spectroscopy: analysis of an isolated beta-sheet model system.lld:pubmed
pubmed-article:18345665pubmed:affiliationHeinrich-Heine Universität Düsseldorf, Institut für Physikalische Chemie I, Universitätsstrasse 26.33.O2, 40225 Düsseldorf, Germany.lld:pubmed
pubmed-article:18345665pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18345665pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed