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FEBS Lett. 2003 Nov 27;555(1):116-21.

Translocons, thermodynamics, and the folding of membrane proteins.

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Department of Physiology and Biophysics and the Program in Macromolecular Structure, University of California at Irvine, Med. Sci. I-D346, 92697-4560, Irvine, CA, USA


Recent three-dimensional structures of helical membrane proteins present new challenges for the prediction of structure from amino acid sequence. Membrane proteins reside stably in a thermodynamic free energy minimum after release into the membrane's bilayer fabric from the translocon complex. This means that structure prediction is primarily a problem of physical chemistry. But the folding processes within the translocon must also be considered. A distilled overview of the physical principles of membrane protein stability is presented, and extended to encompass translocon-assisted folding.

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