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10.1016/j.jmb.2014.09.014 http://scihub22266oqcxt.onion/10.1016/j.jmb.2014.09.014 C4339636!4339636!25277655     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Biol 2015 ; 427 (5): 999-1022 Nephropedia Template TP {{tp|p=25277655|t=2015. Mechanisms of integral membrane protein insertion and folding |pdf=|usr=}}{{25277655}} gab.com Text Mechanisms of integral membrane protein insertion and folding JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=25277655 #FOAvip The biogenesis, folding, and structure of ?-helical membrane proteins (MPs) are important to understand because they underlie virtually all physiological processes in cells including key metabolic pathways, such as the respiratory chain and the photosystems, and the transport of solutes and signals across membranes. Nearly all MPs require translocons?often referred to as protein-conducting channels?for proper insertion into their target membrane. Remarkable progress toward understanding the structure and functioning of translocons has been made during the past decade. Here we review and assess this progress critically. All available evidence indicates that MPs are equilibrium structures that achieve their final structural states by folding along thermodynamically controlled pathways. The main challenge for cells is the targeting and membrane insertion of highly hydrophobic amino acid sequences. Targeting and insertion are managed in cells principally by interactions between ribosomes and membrane-embedded translocons. Our review examines the biophysical and biological boundaries of membrane protein insertion and the folding of polytopic membrane proteins in vivo. A theme of the review is the under-appreciated role of basic thermodynamic principles in MP folding and assembly. Thermodynamics not only dictates the final folded structure, it is the driving force for the evolution of the ribosome-translocon system of assembly. We conclude the review with a perspective suggesting a new view of translocon-guided MP insertion. Twit Text FOAVip Mechanisms of integral membrane protein insertion and folding ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=25277655 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25277655 #FOAvip English Wikipedia <ref>{{Cite pmid|25277655}}</ref> Mechanisms of integral membrane protein insertion and folding #MMPMID25277655 Cymer F; von Heijne G; White SH J Mol Biol 2015[Mar]; 427 (5): 999-1022 PMID25277655show ga The biogenesis, folding, and structure of ?-helical membrane proteins (MPs) are important to understand because they underlie virtually all physiological processes in cells including key metabolic pathways, such as the respiratory chain and the photosystems, and the transport of solutes and signals across membranes. Nearly all MPs require translocons?often referred to as protein-conducting channels?for proper insertion into their target membrane. Remarkable progress toward understanding the structure and functioning of translocons has been made during the past decade. Here we review and assess this progress critically. All available evidence indicates that MPs are equilibrium structures that achieve their final structural states by folding along thermodynamically controlled pathways. The main challenge for cells is the targeting and membrane insertion of highly hydrophobic amino acid sequences. Targeting and insertion are managed in cells principally by interactions between ribosomes and membrane-embedded translocons. Our review examines the biophysical and biological boundaries of membrane protein insertion and the folding of polytopic membrane proteins in vivo. A theme of the review is the under-appreciated role of basic thermodynamic principles in MP folding and assembly. Thermodynamics not only dictates the final folded structure, it is the driving force for the evolution of the ribosome-translocon system of assembly. We conclude the review with a perspective suggesting a new view of translocon-guided MP insertion. äMechanisms of integral membrane protein insertion and folding (epmc).pdf DeepDyve Pubget Overpricing