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Fluorescence relaxation spectroscopy in the analysis of macromolecular structure and motion

Published online by Cambridge University Press:  17 March 2009

Rudolf Rigler  and
Måns Ehrenberg
Rudolf Rigler
Affiliation:
Department of Medical Biophysics, Karolinska Institute, 10401 Stockholm 60, Sweden
Måns Ehrenberg
Affiliation:
Department of Medical Biophysics, Karolinska Institute, 10401 Stockholm 60, Sweden
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Extract

Fluorescence spectroscopy offers particularly sensitive tools for the investigation of physical properties of macromolecules in solution. Differences in molecular structure under varying experimental conditions are often reflected in quantum yield and lifetime of natural or synthetically inserted fluorescent probes. inserted fluorescent probes. Energy transfer between fluorescent groups at known places of a primary sequence can be used to measure distances between the label sites (Eisinger, 1976) as well as to investigate their relative motion, e.g. measurements of the kinetics of variations in the end to end distance of a polymer (E. Haas & I. Steinberg, personal communication).

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 9 , Issue 1 , February 1976 , pp. 1 - 19
Copyright
Copyright © Cambridge University Press 1976

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