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Topics in Fluorescence Spectroscopy pp 113–136Cite as

Tryptophan Phosphorescence from Proteins at Room Temperature

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Part of the book series: Topics in Fluorescence Spectroscopy ((TIFS,volume 3))

Conclusions

Phosphorescence is readily detectable from most types of proteins at room temperature. Tryptophan phosphorescence lifetimes and yields are very sensitive to environment, and therefore phosphorescence is sensitive to conformational changes in proteins. Fundamental questions concerning exactly what parameters affect lifetime and spectra of tryptophan in proteins remain still to be answered.

The long lifetime of phosphorescence allows it to be used for processes which are slow-on the millisecond to microsecond time scale. Among these processes are the turnover time of enzymes and diffusion of large aggregates or smaller proteins in a restricted environment, such as, for example, proteins in membranes. Phosphorescence anisotropy is one method to study these processes, giving information on rotational diffusion. Quenching by external molecules is another potentially powerful method; in this case it can lead to information on tryptophan location and the structural dynamics of the protein.

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  1. Department of Biochemistry and Biophysics, School of Medicine University of Pennsylvania, Philadelphia, Pennsylvania, 19104, USA

    Jane M. Vanderkooi

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  1. Center for Fluorescence Spectroscopy Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore, Maryland, USA

    Joseph R. Lakowicz

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Vanderkooi, J.M. (2002). Tryptophan Phosphorescence from Proteins at Room Temperature. In: Lakowicz, J.R. (eds) Topics in Fluorescence Spectroscopy. Topics in Fluorescence Spectroscopy, vol 3. Springer, Boston, MA. https://doi.org/10.1007/0-306-47059-4_3

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