Determining the Free Energies of Outer Membrane Proteins in Lipid Bilayers. Academic Article uri icon

Overview

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.

publication date

  • January 1, 2020

Research

keywords

  • Bacterial Outer Membrane Proteins
  • Escherichia coli
  • Escherichia coli Proteins
  • Lipid Bilayers
  • Protein Folding
  • Thermodynamics

Identity

Scopus Document Identifier

  • 85101492752

Digital Object Identifier (DOI)

  • 10.1002/mabi.200900479

PubMed ID

  • 33582994

Additional Document Info

volume

  • 2168