Literature DB >> 19459617

Equilibrium exchange processes of the aqueous tryptophan dipeptide.

Sayan Bagchi1, Adam K Charnley, Amos B Smith Iii, Robin M Hochstrasser.   

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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Year:  2009        PMID： 19459617      PMCID： PMC2929808          DOI： 10.1021/jp811168x

Source DB:  PubMed          Journal:  J Phys Chem B        ISSN： 1520-5207            Impact factor:   2.991


  34 in total

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