Optical Spectroscopy of Membrane Protein/Amphipol Complexes

Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)


Most optical spectroscopy approaches can be applied to membrane protein/amphipol (MP/APol) complexes, namely UV-visible absorbance spectroscopy, light scattering, circular dichroism, static and time-resolved fluorescence measurements, fluorescence quenching and Förster resonance energy transfer studies, surface plasmon resonance measurements, etc. A notable exception is infrared absorbance studies in the peptide bond absorbance bands. Indeed, most APols comprise amide bonds, in which case absorbance spectroscopy studies of APol-trapped MPs at the peptide bond wavelengths have proven intractable. Resonance Raman studies however are possible, as well as surface-enhanced Raman spectroscopy.

A large number of APols carrying fluorescent labels have been developed, opening the way to a vast range of applications, from the study of the composition, organization, and dynamics of MP/APol complexes to topological and conformational studies of MPs and to imaging of the distribution and elimination of APols in cell cultures and live animals.


Surface-enhanced Raman Scattering Absorbance Spectroscopy Förster Resonance Energy Transfer Synchrotron Radiation Circular Dichroism (SRCD) Amphipols 
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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Authors and Affiliations

  1. 1.Institut de Biologie Physico-ChimiqueParisFrance

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