Table of Contents
Journal of Amino Acids
Volume 2012, Article ID 735076, 10 pages
http://dx.doi.org/10.1155/2012/735076
Research Article

Correlation of TrpGly and GlyTrp Rotamer Structure with W7 and W10 UV Resonance Raman Modes and Fluorescence Emission Shifts

Department of Chemistry, Brooklyn College of the City University of New York, 2900 Bedford Avenue, Brooklyn, NY 11210, USA

Received 30 March 2012; Accepted 4 May 2012

Academic Editor: Hieronim Jakubowski

Copyright © 2012 Azaria Solomon Eisenberg and Laura J. Juszczak. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Tryptophyl glycine (TrpGly) and glycyl tryptophan (GlyTrp) dipeptides at pH 5.5 and pH 9.3 show a pattern of fluorescence emission shifts with the TrpGly zwitterion emission solely blue shifted. This pattern is matched by shifts in the UV resonance Raman (UVRR) W10 band position and the W7 Fermi doublet band ratio. Ab initio calculations show that the 1340 cm−1 band of the W7 doublet is composed of three modes, two of which determine the W7 band ratios for the dipeptides. Molecular dynamics simulations show that the dipeptides take on two conformations: one with the peptide backbone extended; one with the backbone curled over the indole. The dihedral angle critical to these conformations is χ1 and takes on three discrete values. Only the TrpGly zwitterion spends an appreciable amount of time in the extended backbone conformation as this is stabilized by two hydrogen bonds with the terminal amine cation. According to a Stark effect model, a positive charge near the pyrrole keeps the 1La transition at high energy, limiting fluorescence emission red shift, as observed for the TrpGly zwitterion. The hydrogen bond stabilized backbone provides a rationale for the Cmethylene-Cα-Ccarbonyl W10 symmetric stretch that is unique to the TrpGly zwitterion.