Equilibrium exchange processes of the aqueous tryptophan dipeptide

J Phys Chem B. 2009 Jun 18;113(24):8412-7. doi: 10.1021/jp811168x.

Abstract

The tryptophan dipeptide (NATMA) in D2O shows two conformers having distinctive acetyl end amide-I' transition frequencies. In 2D echo spectroscopy, cross peaks between these conformer transitions are used to show that they are undergoing exchange on the 1.5 ps time scale. Simulations suggest that the accessibility of the amide group to water is restricted in one of the conformations.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computer Simulation
  • Deuterium Oxide / chemistry*
  • Dipeptides / chemistry*
  • Models, Chemical
  • Spectrophotometry, Infrared
  • Tryptophan / chemistry*

Substances

  • Dipeptides
  • Tryptophan
  • Deuterium Oxide