Journal
PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES
Volume 7, Issue 11, Pages 1301-1312Publisher
SPRINGERNATURE
DOI: 10.1039/b804450n
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM076665] Funding Source: NIH RePORTER
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Time-resolved fluorescence spectroscopy is an indispensable tool in the chemical, physical and biological sciences for the study of fast kinetic processes in the subpicosecond to microsecond time scale. This review focuses on the development and modern implementation of the frequency domain approach to time-resolved fluorescence. Both intensity decay (lifetime) and anisotropy decay (dynamic polarization) will be considered and their application to intrinsic protein fluorescence will be highlighted. In particular we shall discuss the photophysics of the aromatic amino acids, tryptophan, tyrosine and phenylalanine, which are responsible for intrinsic protein fluorescence. This discussion will be illustrated with examples of frequency domain studies on several protein systems.
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