Fluorescence polarization analysis of protein-DNA and protein-protein interactions.
Author(s) -
James R. Lundblad,
Megan E. Laurance,
Richard H. Goodman
Publication year - 1996
Publication title -
molecular endocrinology
Language(s) - English
Resource type - Journals
eISSN - 1944-9917
pISSN - 0888-8809
DOI - 10.1210/mend.10.6.8776720
Subject(s) - biology , fluorescence anisotropy , dna , fluorescence , protein–protein interaction , macromolecule , biophysics , polarization (electrochemistry) , förster resonance energy transfer , computational biology , biochemistry , chemistry , physics , quantum mechanics , membrane
Fluorescence polarization is a powerful technique for characterizing macromolecular associations and can provide equilibrium determinations of protein-DNA and protein-protein interactions. This technique is particularly useful (and better suited than electrophoretic methods) to study low affinity protein-protein interactions. In this review, we have outlined the principles underlying the use of fluorescence polarization to study the assembly of higher order complexes that bind to the CRE. The availability of simple, relatively inexpensive instrumentation means that this technology is no longer only within the realm of the physical biochemist.
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