Gutenberg Open Science: Sequence-specific dimerization of a transmembrane helix in amphipol A8-35

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-7845

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DC Field	Value	Language
dc.contributor.author	Stangl, Michael	-
dc.contributor.author	Unger, Sebastian	-
dc.contributor.author	Keller, Sandro	-
dc.contributor.author	Schneider, Dirk	-
dc.date.accessioned	2022-10-05T08:57:39Z	-
dc.date.available	2022-10-05T08:57:39Z	-
dc.date.issued	2014
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/7860	-
dc.description.abstract	As traditional detergents might destabilize or even denature membrane proteins, amphiphilic polymers have moved into the focus of membrane-protein research in recent years. Thus far, Amphipols are the best studied amphiphilic copolymers, having a hydrophilic backbone with short hydrophobic chains. However, since stabilizing as well as destabilizing effects of the Amphipol belt on the structure of membrane proteins have been described, we systematically analyze the impact of the most commonly used Amphipol A8-35 on the structure and stability of a well-defined transmembrane protein model, the glycophorin A transmembrane helix dimer. Amphipols are not able to directly extract proteins from their native membranes, and detergents are typically replaced by Amphipols only after protein extraction from membranes. As Amphipols form mixed micelles with detergents, a better understanding of Amphipol-detergent interactions is required. Therefore, we analyze the interaction of A8-35 with the anionic detergent sodium dodecyl sulfate and describe the impact of the mixed-micelle-like system on the stability of a transmembrane helix dimer. As A8-35 may highly stabilize and thereby rigidify a transmembrane protein structure, modest destabilization by controlled addition of detergents and formation of mixed micellar systems might be helpful to preserve the function of a membrane protein in Amphipol environments.	en_GB
dc.description.sponsorship	DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin	de
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	500 Naturwissenschaften	de_DE
dc.subject.ddc	500 Natural sciences and mathematics	en_GB
dc.title	Sequence-specific dimerization of a transmembrane helix in amphipol A8-35	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-7845	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 09 Chemie, Pharmazie u. Geowissensch.	de
jgu.organisation.number	7950	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	PLoS one	de
jgu.journal.volume	9	de
jgu.journal.issue	10	de
jgu.pages.alternative	e110970	de
jgu.publisher.year	2014	-
jgu.publisher.name	PLoS	de
jgu.publisher.place	Lawrence, Kan.	de
jgu.publisher.uri	http://dx.doi.org/10.1371/journal.pone.0110970	de
jgu.publisher.issn	1932-6203	de
jgu.organisation.place	Mainz	-
jgu.identifier.pmid	25347769
jgu.subject.ddccode	500	de
opus.date.modified	2018-08-08T09:24:24Z
opus.subject.dfgcode	00-000
opus.organisation.string	FB 09: Chemie, Pharmazie und Geowissenschaften: Institut für Pharmazie	de_DE
opus.identifier.opusid	50061
opus.importsource	pubmed
opus.institute.number	0908
opus.metadataonly	false
opus.type.contenttype	Keine	de_DE
opus.type.contenttype	None	en_EN
opus.affiliated	Stangl, Michael
opus.affiliated	Schneider, Dirk
jgu.publisher.doi	10.1371/journal.pone.0110970	de
jgu.organisation.ror	https://ror.org/023b0x485	-
Appears in collections:	DFG-OA-Publizieren (2012 - 2017)

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