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Published on: February 21, 2019
Determining the Free Energies of Outer Membrane Proteins in Lipid Bilayers
Gerard H M Huysmans1, Dagan C Marx2, Sheena E Radford3
1Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY, USA. ghh2001@med.cornell.edu.
Abstract:
The thermodynamic stabilities of membrane proteins are of fundamental interest to provide a biophysical description of their structure-function relationships because energy determines conformational populations. In addition, structure-energy relationships can be exploited in membrane protein design and in synthetic biology. To determine the thermodynamic stability of a membrane protein, it is not sufficient to be able to unfold and refold the molecule: establishing path independence of this reaction is essential. Here we describe the procedures required to measure and verify path independence for the folding of outer membrane proteins in large unilamellar vesicles.
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