Literature DB >> 10527728

Quantification of protein-protein interactions using fluorescence polarization.

D M Jameson1, S E Seifried.   

Abstract

Quantitative determinations of the dissociation constants of biomolecular interactions, in particular protein-protein interactions, are essential for a detailed understanding of the molecular basis of their specificities. Fluorescence spectroscopy is particularly well suited for such studies. This article highlights the theoretical and practical aspects of fluorescence polarization and its application to the study of protein-protein interactions. Consideration is given to the nature of the different types of fluorescence probes available and the probe characteristics appropriate for the system under investigation. Several examples from the literature are discussed that illustrate different practical aspects of the technique applied to diverse systems. Copyright 1999 Academic Press.

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Year:  1999        PMID: 10527728     DOI: 10.1006/meth.1999.0853

Source DB:  PubMed          Journal:  Methods        ISSN: 1046-2023            Impact factor:   3.608


  25 in total

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5.  Nox4 B-loop creates an interface between the transmembrane and dehydrogenase domains.

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6.  Interrogation of MDM2 phosphorylation in p53 activation using native chemical ligation: the functional role of Ser17 phosphorylation in MDM2 reexamined.

Authors:  Changyou Zhan; Kristen Varney; Weirong Yuan; Le Zhao; Wuyuan Lu
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7.  Studies on the dissociation and urea-induced unfolding of FtsZ support the dimer nucleus polymerization mechanism.

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Review 8.  Biophysical characterization of recombinant proteins: a key to higher structural genomics success.

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9.  Total chemical synthesis of dengue 2 virus capsid protein via native chemical ligation: role of the conserved salt-bridge.

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10.  Magnesium coordination controls the molecular switch function of DNA mismatch repair protein MutS.

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Journal:  J Biol Chem       Date:  2010-02-18       Impact factor: 5.157

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