It is proposed that membrane proteins fold spontaneously inside of the cell membrane to adopt the structures that allow them to carry out their function. These membranes primarily consist of fatty molecules called lipids, but they are also packed with proteins such as ion channels and transporters that control which molecules pass in and out of the cell.
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This allows for the measurement of the free energy of ClC-ec1 dimerization in lipid bilayers, revealing that it is one of the strongest membrane protein complexes measured so far, and introduces it as new type of dimerization model to investigate the physical forces that drive membrane protein association in membranes.Ĭells are encapsulated by membranes that form a barrier between the inside of the cell and the outside world. The capture statistics describe a monomer to dimer transition that is dependent on the subunit/lipid mole fraction density and follows an equilibrium dimerization isotherm. Here, we use single-molecule photobleaching analysis to measure the probability of ClC-ec1 subunit capture into liposomes during extrusion of large, multilamellar membranes. Studying dimerization of ClC-type transporters offers a new approach to the problem, as individual subunits adopt a stable and functionally verifiable fold that constrains the system to two states – monomer or dimer. Interactions between membrane protein interfaces in lipid bilayers play an important role in membrane protein folding but quantification of the strength of these interactions has been challenging.
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