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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
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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. |
format | Online Article Text |
id | pubmed-4303321 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT danoffemilyj membranedefectsaccelerateoutermembranebbarrelproteinfolding AT flemingkareng membranedefectsaccelerateoutermembranebbarrelproteinfolding |