Probing Membrane Protein Structure and Dynamics by Fluorescence Spectroscopy
Peptides and Proteins
Published Online: 18 SEP 2013
Copyright © 2000 John Wiley & Sons, Ltd. All rights reserved.
Encyclopedia of Analytical Chemistry
How to Cite
Kang, G., López-Peña, I., Bhakta, S. and Kim, J. E. 2013. Probing Membrane Protein Structure and Dynamics by Fluorescence Spectroscopy. Encyclopedia of Analytical Chemistry. 1–21.
- Published Online: 18 SEP 2013
Applications of fluorescence spectroscopy to biomolecules, with focus on membrane proteins, are discussed in this article. A broad range of molecular insights can be gained with this simple technique because the emission properties of a chromophore are typically sensitive to the environment. The intensities and maximum wavelengths of steady-state fluorescence spectra are used to elucidate the thermodynamics of membrane protein folding, monitor the extent of solvent exposure of chromophores, determine the depths of insertion into synthetic bilayers, probe the degree of rotational freedom in solvent-exposed and buried regions, and measure the evolution of distances between donor and acceptor moieties. We also address some of the challenges associated with fluorescence measurements of integral membrane proteins. An important goal is to provide a practical guide for laboratory measurements as well as examples of analyses related to membrane protein structure and dynamics.