Equilibrium exchange processes of the aqueous tryptophan dipeptide
Sayan Bagchi1, Adam K Charnley, Amos B Smith Iii
1Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, USA.
The Journal of Physical Chemistry. B
|May 23, 2009
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.
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