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  • Title: The dead-end elimination method, tryptophan rotamers, and fluorescence lifetimes.
    Author: Hellings M, De Maeyer M, Verheyden S, Hao Q, Van Damme EJ, Peumans WJ, Engelborghs Y.
    Journal: Biophys J; 2003 Sep; 85(3):1894-902. PubMed ID: 12944302.
    Abstract:
    The Dead-End Elimination method was used to identify 40 low energy microconformations of 16 tryptophan residues in eight proteins. Single Trp-mutants of these proteins all show a double- or triple-exponential fluorescence decay. For ten of these lifetimes the corresponding rotameric state could be identified by comparing the bimolecular acrylamide quenching constant (k(q)) and the relative solvent exposure of the side chain in that microstate. In the absence of any identifiable quencher, the origin of the lifetime heterogeneity is interpreted in terms of the electron transfer process from the indole C epsilon 3 atom to the carbonyl carbon of the peptide bond. Therefore it is expected that a shorter [C epsilon 3-C[double bond]O] distance leads to a shorter lifetime as observed for these ten rotamers. Applying the same rule to the other 30 lifetimes, a link with their corresponding rotameric state could also be made. In agreement with the theory of Marcus and Sutin, the nonradiative rate constant shows an exponential relationship with the [C epsilon 3-C[double bond]O] distance for the 40 datapoints.
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