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• W2014591465 abstract "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." @default.
• W2014591465 created "2016-06-24" @default.
• W2014591465 creator A5053094051 @default.
• W2014591465 date "2003-10-15" @default.
• W2014591465 modified "2023-10-14" @default.
• W2014591465 title "Translocons, thermodynamics, and the folding of membrane proteins" @default.
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• W2014591465 doi "https://doi.org/10.1016/s0014-5793(03)01153-0" @default.
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