Abstract
The fluorescence of proteins is often dominated by that of the tryptophan residues, and the fluorescence properties of individual tryptophan residues are strongly influenced by their different microenvironments. This has been widely exploited in the use of tryptophan as an intrinsic probe for the structure and conformation of proteins and polypeptides in solution. The usefulness of such a probe is based on the implicit assumption that the fluorescence of an isolated tryptophan decays mono-exponentially.
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Beddard, G.S. (1983). The Photophysics of Tryptophan. In: Cundall, R.B., Dale, R.E. (eds) Time-Resolved Fluorescence Spectroscopy in Biochemistry and Biology. NATO Advanced Science Institutes Series, vol 69. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1634-4_35
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DOI: https://doi.org/10.1007/978-1-4757-1634-4_35
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