Translocons, thermodynamics, and the folding of membrane proteins.
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.
White
Stephen H
SH
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
D002135:Calcium-Binding Proteins / Q000737:chemistry*; D004734:Energy Metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000737:chemistry; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry*; D018000:Receptors, Peptide / Q000737:chemistry*; D013816:Thermodynamics
D002135:Calcium-Binding Proteins; D008051:Lipid Bilayers; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D018160:Receptors, Cytoplasmic and Nuclear; D018000:Receptors, Peptide; C066973:signal sequence receptor