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Proceedings Paper

Use Of Nanosecond Pulse Fluorimetry For The Study Of Protein Structure
Author(s): R. M. Dowben; G. Lin
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Paper Abstract

Nanosecond pulse fluorescent spectroscopy is a very powerful method for studying protein structure in solution. Studies using this methodology fall into two main categories, measurement of the decay of total fluorescence to evaluate fluorescence lifetime, and time-resolved fluorescence anisotropy measurements of the decay of polarization. The experiments are performed by attaching fluorescent probes to various known sites on protein molecules. The lifetime experiments tell us about the dynamic properties of the fluorescent moiety itself, while the anisotropy measurements provide information about the shape and hydrodynamic properties of the protein to which the fluorescent moiety is attached. Fluorescent probes that show only simple fluorescence can be used for studies with lifetimes up to about 120 ns; probes that form triplets will have longer lifetimes into the microsecond or even millisecond range.

Paper Details

Date Published: 1 January 1987
PDF: 4 pages
Proc. SPIE 0743, Fluorescence Detection, (1 January 1987); doi: 10.1117/12.966936
Show Author Affiliations
R. M. Dowben, University of Texas Health Science Center (United States)
G. Lin, University of Texas Health Science Center (United States)


Published in SPIE Proceedings Vol. 0743:
Fluorescence Detection
E. Roland Menzel, Editor(s)

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