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Biophys J. 2001 May;80(5):2093-109.

Mechanisms of tryptophan fluorescence shifts in proteins.

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1
Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, USA.

Abstract

Tryptophan fluorescence wavelength is widely used as a tool to monitor changes in proteins and to make inferences regarding local structure and dynamics. We have predicted the fluorescence wavelengths of 19 tryptophans in 16 proteins, starting with crystal structures and using a hybrid quantum mechanical-classical molecular dynamics method with the assumption that only electrostatic interactions of the tryptophan ring electron density with the surrounding protein and solvent affect the transition energy. With only one adjustable parameter, the scaling of the quantum mechanical atomic charges as seen by the protein/solvent environment, the mean absolute deviation between predicted and observed fluorescence maximum wavelength is 6 nm. The modeling of electrostatic interactions, including hydration, in proteins is vital to understanding function and structure, and this study helps to assess the effectiveness of current electrostatic models.

PMID:
11325713
PMCID:
PMC1301402
DOI:
10.1016/S0006-3495(01)76183-8
[Indexed for MEDLINE]
Free PMC Article
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