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Novel Tripod Amphiphiles for Membrane Protein Analysis

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dc.contributor.authorChae, Pil Seok-
dc.contributor.authorKruse, Andrew C.-
dc.contributor.authorGotfryd, Kamil-
dc.contributor.authorRana, Rohini R.-
dc.contributor.authorCho, Kyung Ho-
dc.contributor.authorRasmussen, Soren G. F.-
dc.contributor.authorBae, Hyoung Eun-
dc.contributor.authorChandra, Richa-
dc.contributor.authorGether, Ulrik-
dc.contributor.authorGuan, Lan-
dc.contributor.authorKobilka, Brian K.-
dc.contributor.authorLoland, Claus J.-
dc.contributor.authorByrne, Bernadette-
dc.contributor.authorGellman, Samuel H.-
dc.date.accessioned2021-06-23T02:04:10Z-
dc.date.available2021-06-23T02:04:10Z-
dc.date.created2021-01-21-
dc.date.issued2013-11-
dc.identifier.issn0947-6539-
dc.identifier.urihttps://scholarworks.bwise.kr/erica/handle/2021.sw.erica/26314-
dc.description.abstractIntegral membrane proteins play central roles in controlling the flow of information and molecules across membranes. Our understanding of membrane protein structures and functions, however, is seriously limited, mainly due to difficulties in handling and analysing these proteins in aqueous solution. The use of a detergent or other amphipathic agents is required to overcome the intrinsic incompatibility between the large lipophilic surfaces displayed by the membrane proteins in their native forms and the polar solvent molecules. Here, we introduce new tripod amphiphiles displaying favourable behaviours toward several membrane protein systems, leading to an enhanced protein solubilisation and stabilisation compared to both conventional detergents and previously described tripod amphiphiles.-
dc.language영어-
dc.language.isoen-
dc.publisherJohn Wiley & Sons Ltd.-
dc.titleNovel Tripod Amphiphiles for Membrane Protein Analysis-
dc.typeArticle-
dc.contributor.affiliatedAuthorChae, Pil Seok-
dc.identifier.doi10.1002/chem.201301423-
dc.identifier.scopusid2-s2.0-84887022427-
dc.identifier.wosid000326311400030-
dc.identifier.bibliographicCitationChemistry - A European Journal, v.19, no.46, pp.15645 - 15651-
dc.relation.isPartOfChemistry - A European Journal-
dc.citation.titleChemistry - A European Journal-
dc.citation.volume19-
dc.citation.number46-
dc.citation.startPage15645-
dc.citation.endPage15651-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalWebOfScienceCategoryChemistry, Multidisciplinary-
dc.subject.keywordPlusSTRUCTURAL INSIGHTS-
dc.subject.keywordPlusFACIAL AMPHIPHILES-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusMNG AMPHIPHILES-
dc.subject.keywordPlusRECEPTOR-
dc.subject.keywordPlusSOLUBILIZATION-
dc.subject.keywordPlusSTABILIZATION-
dc.subject.keywordPlusSURFACTANTS-
dc.subject.keywordPlusDETERGENTS-
dc.subject.keywordPlusSTABILITY-
dc.subject.keywordAuthoramphiphiles-
dc.subject.keywordAuthormembrane proteins-
dc.subject.keywordAuthormolecular design-
dc.subject.keywordAuthorprotein structures-
dc.subject.keywordAuthorstabilization-
dc.identifier.urlhttps://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.201301423-
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ERICA 공학대학 (DEPARTMENT OF BIONANO ENGINEERING)
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