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dc.contributor.author채필석-
dc.date.accessioned2019-04-10T05:26:59Z-
dc.date.available2019-04-10T05:26:59Z-
dc.date.issued2016-12-
dc.identifier.citationCHEMISTRY-A EUROPEAN JOURNAL, v. 22, NO. 52, Page. 18833-18839en_US
dc.identifier.issn0947-6539-
dc.identifier.issn1521-3765-
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/full/10.1002/chem.201603338-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/101666-
dc.description.abstractDetergents serve as useful tools for membrane protein structural and functional studies. Their amphipathic nature allows detergents to associate with the hydrophobic regions of membrane proteins whilst maintaining the proteins in aqueous solution. However, widely used conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus there are major efforts underway to develop novel agents with improved properties. We prepared mesitylene-cored glucoside amphiphiles (MGAs) with three alkyl chains and compared these agents with previously developed xylene-linked malto-side agents (XMAs) with two alkyl chains and a conventional detergent (DDM). When these agents were evaluated for four membrane proteins including a G protein-coupled receptor (GPCR), some agents such as MGA-C13 and MGA-C14 resulted in markedly enhanced stability of membrane proteins compared to both DDM and the XMAs. This favourable behaviour is due likely to the increased hydrophobic density provided by the extra alkyl chain. Thus, this study not only describes new glucoside agents with potential for membrane protein research, but also introduces a new detergent design principle for future development.en_US
dc.description.sponsorshipThis work was supported by the National Research Foundation of Korea (NRF) funded by the Korean government (MSIP) (grant number 2008-0061891 and 2016R1A2B2011257 to P.S.C. and K.H.C.). This work was also supported by the National Science Foundation (grant number: MCB-1158085 to L.G.) and by the National Institutes of Health (grant number: R01 GM095538 to L.G.).en_US
dc.language.isoenen_US
dc.publisherWILEY-V C H VERLAG GMBHen_US
dc.subjectamphiphile designen_US
dc.subjectdetergentsen_US
dc.subjectmembrane proteinsen_US
dc.subjectprotein solubilisationen_US
dc.subjectprotein stabilizationen_US
dc.titleMesitylene-Cored Glucoside Amphiphiles (MGAs) for Membrane Protein Studies: Importance of Alkyl Chain Density in Detergent Efficacyen_US
dc.typeArticleen_US
dc.relation.no52-
dc.relation.volume22-
dc.identifier.doi10.1002/chem.201603338-
dc.relation.page18833-18839-
dc.relation.journalCHEMISTRY-A EUROPEAN JOURNAL-
dc.contributor.googleauthorCho, Kyung Ho-
dc.contributor.googleauthorRibeiro, Orquidea-
dc.contributor.googleauthorDu, Yang-
dc.contributor.googleauthorTikhonova, Elena-
dc.contributor.googleauthorMortensen, Jonas S.-
dc.contributor.googleauthorMarkham, Kelsey-
dc.contributor.googleauthorHariharan, Parameswaran-
dc.contributor.googleauthorLoland, Claus J.-
dc.contributor.googleauthorGuan, Lan-
dc.contributor.googleauthorChae, Pil Seok-
dc.relation.code2016002476-
dc.sector.campusS-
dc.sector.daehakGRADUATE SCHOOL[S]-
dc.sector.departmentDEPARTMENT OF BIONANOTECHNOLOGY-
dc.identifier.pidpchae-
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GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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