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Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding

[Image: see text] Outer membrane β-barrel proteins spontaneously fold into lipid bilayers with rates of folding that are strongly influenced by the physical properties of the membrane. We show that folding is accelerated when the bilayer is at the phase transition temperature, because of the coexist...

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Autores principales: Danoff, Emily J., Fleming, Karen G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4303321/
https://www.ncbi.nlm.nih.gov/pubmed/25513891
http://dx.doi.org/10.1021/bi501443p
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author Danoff, Emily J.
Fleming, Karen G.
author_facet Danoff, Emily J.
Fleming, Karen G.
author_sort Danoff, Emily J.
collection PubMed
description [Image: see text] Outer membrane β-barrel proteins spontaneously fold into lipid bilayers with rates of folding that are strongly influenced by the physical properties of the membrane. We show that folding is accelerated when the bilayer is at the phase transition temperature, because of the coexistence of lipid phase domains and the high degree of defects present at domain boundaries. These results are consistent with previous observations of faster folding into thin and highly curved membranes, which also contain a higher prevalence of defects. The importance of defects in β-barrel folding provides insight into the intrinsic folding process and the biological assembly pathway.
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spelling pubmed-43033212015-12-16 Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding Danoff, Emily J. Fleming, Karen G. Biochemistry [Image: see text] Outer membrane β-barrel proteins spontaneously fold into lipid bilayers with rates of folding that are strongly influenced by the physical properties of the membrane. We show that folding is accelerated when the bilayer is at the phase transition temperature, because of the coexistence of lipid phase domains and the high degree of defects present at domain boundaries. These results are consistent with previous observations of faster folding into thin and highly curved membranes, which also contain a higher prevalence of defects. The importance of defects in β-barrel folding provides insight into the intrinsic folding process and the biological assembly pathway. American Chemical Society 2014-12-16 2015-01-20 /pmc/articles/PMC4303321/ /pubmed/25513891 http://dx.doi.org/10.1021/bi501443p Text en Copyright © 2014 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Danoff, Emily J.
Fleming, Karen G.
Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding
title Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding
title_full Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding
title_fullStr Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding
title_full_unstemmed Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding
title_short Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding
title_sort membrane defects accelerate outer membrane β-barrel protein folding
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4303321/
https://www.ncbi.nlm.nih.gov/pubmed/25513891
http://dx.doi.org/10.1021/bi501443p
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