Resonance-Enhanced Multiphoton lonization Spectroscopy of Dipeptides

Kami Cohen, Beth Brauer, Eyal Nir, Louis Grace, Mattanjah S. De Vries

Research output: Contribution to journalArticlepeer-review

96 Scopus citations

Abstract

We report resonance-enhanced multiphoton ionization (REMPI) spectroscopy of laser-desorbed, jet-cooled dipeptides, containing either tyrosine or phenylalanine as an aromatic chromophore (C). The single amino acids have multiple origins that we interpret as arising from two types of conformations, with the carboxyl group either anti or gauche with respect to the ring. Spectra for dipeptides of the form X-C, for example, Ala-Tyr, are similar to those of the corresponding single amino acid. On the other hand, spectra for dipeptides of the form C-X, for example, Tyr-Ala, show significant changes in the peaks, which we associate with gauche conformations. This observation can be understood in terms of an interaction between the carboxyl terminus and the ring, associated with the molecule assuming a folded conformation.

Original languageEnglish
Pages (from-to)6351-6355
Number of pages5
JournalJournal of Physical Chemistry A
Volume104
Issue number27
DOIs
StatePublished - 1 Jan 2000
Externally publishedYes

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