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Exploring the Electrostatic Landscape of Proteins with Tryptophan Fluorescence

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Reviews in Fluorescence 2007

Part of the book series: Reviews in Fluorescence ((RFLU,volume 2007))

Abstract

The objective of this review is to present information gained during the last decade that has transformed tryptophan (Trp) into a well-understood fluorescent probe—a probe with no more complications than most non-intrinsic probes, which are usually large dyes with incompletely explored complexity. An overview highlights and summarizes key advancements during the last decade that have increased our understanding of Trp and its fluorescence in proteins. This is followed by sections devoted to (1) the understanding of quenching (mostly caused by electron transfer for which there has been considerable progress), (2) the prediction of steady state fluorescence wavelengths in proteins, (3) nonexponential decay (which remains challenging), and (4) a section that catalogs a number of fundamental experiments and computations on the isolated Trp chromophore that have provided much of the infrastructure for the preceding sections. There is continual emphasis in this chapter on the simple—yet accurate—concept that the extremes of electrostatic fields in proteins are mirrored in the variability and sensitivity of Trp fluorescence quantum yields, lifetimes, and wavelengths.

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    Patrik R. Callis

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Callis, P.R. (2009). Exploring the Electrostatic Landscape of Proteins with Tryptophan Fluorescence. In: Reviews in Fluorescence 2007. Reviews in Fluorescence, vol 2007. Springer, New York, NY. https://doi.org/10.1007/978-0-387-88722-7_10

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