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Spectroscopic Probes for Conformational Transients of Membrane Proteins

  • R. Wagner
Part of the NATO ASI Series book series (NSSA, volume 91)

Abstract

Energy transduction in biological membranes is supported by functionally distinct protein complexes embedded in the lipid bilayer matrix. Various biophysical methods introduced to the field of biomembranes yielded indispensible information about structure and function of the lipid bilayers and their embedded protein complexes. The demonstration of the lateral and rotational mobility of membrane proteins (1,2) undoubtedly influenced the current concepts of membrane structure and function to a large extent. In principle there are three main methods which can yield quantitative information on lateral and rotational mobility of membrane proteins. These are: fluorescence, phosphorescence, and absorption polarization techniques; fluorescence photobleaching recovery; and saturation transfer in electron parametric resonance (for reviews see 3,4). Here the use of phosphorescence (triplet) probes for measuring the rotational diffusion of intrinsic and extrinsic membrane proteins will be described. Besides yielding information on internal fluctuations within the protein, this technique enables the measurement of comparatively slow rotational diffusion (> 0.1 Pa s = 1 cp), i.e., in biological membranes. Thus it extends the application range to time domains which are more relevant to the biological action of enzymes.

Keywords

Triplet State Rotational Motion Rotational Diffusion Rotational Correlation Time Rotational Mobility 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • R. Wagner
    • 1
  1. 1.Biophysics Department of Biologie/ChemistryUniversity of OsnabrueckOsnabrueckGermany

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