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Azaria Solomon Eisenberg and Laura J. Juszczak Relating Trp-Glu dipeptide fluorescence to molecular conformation: The role of the discrete chi 1 and chi 2 angles Journal of Computational Chemistry 34

Version of Record online: 8 APR 2013 | DOI: 10.1002/jcc.23288

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Molecular dynamics simulation reveals the effect of the Trp-Glu charge state on dipeptide conformation preferences. Two general conformations are found, including one where the backbone stretches away from the indole ring, as shown here. The consequence of a “backbone-stretched” conformation is noncovalent interaction between the terminal amine cation and indole ring. Using this and other theoretical data, trends in tryptophan fluorescence maxima and lifetimes for different dipeptide species can be explained.

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