Translocons, thermodynamics, and the folding of membrane proteins

FEBS Letters

White, Stephen H.¹ 

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

关键词: Integral membrane protein;    Protein folding;    Structure prediction;    MP;    membrane protein;    TM;    transmembrane;    HC;    hydrocarbon core of a lipid bilayer;    IF;    interfacial region of a lipid bilayer;    PC;    phosphatidylcholine;    POPC;    palmitoyloleoylphosphatidylcholine;    WW;    Wimley–White;   

DOI  :  10.1016/S0014-5793(03)01153-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown