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dc.contributor.author채필석-
dc.date.accessioned2016-12-12T05:32:02Z-
dc.date.available2016-12-12T05:32:02Z-
dc.date.issued2015-05-
dc.identifier.citationANALYST, v. 140, NO 9, Page. 3157-3163en_US
dc.identifier.issn0003-2654-
dc.identifier.issn1364-5528-
dc.identifier.urihttp://pubs.rsc.org/en/Content/ArticleLanding/2015/AN/C5AN00240K#!divAbstract-
dc.identifier.urihttp://hdl.handle.net/20.500.11754/24791-
dc.description.abstractDetergents are typically used to both extract membrane proteins (MPs) from the lipid bilayers and maintain them in solution. However, MPs encapsulated in detergent micelles are often prone to denaturation and aggregation. Thus, the development of novel agents with enhanced stabilization characteristics is necessary to advance MP research. Maltose neopentyl glycol-3 (MNG-3) has contributed to ˃10 crystal structures including G-protein coupled receptors. Here, we prepared MNG-3 analogues and characterised their properties using selected MPs. Most MNGs were superior to a conventional detergent, n-dodecyl-beta-D-maltopyranoside (DDM), in terms of membrane protein stabilization efficacy. Interestingly, optimal stabilization was achieved with different MNG-3 analogues depending on the target MP. The origin for such detergent specificity could be explained by a novel concept: compatibility between detergent hydrophobicity and MP tendency to denature and aggregate. This set of MNGs represents viable alternatives to currently available detergents for handling MPs, and can be also used as tools to estimate MP sensitivity to denaturation and aggregation.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 2013R1A2A2A03067623 to P.S.C., K.H.C, H.J.L. and J.G.), Biotechnology and Biological Sciences Research Council (grant BB/K017292/1) to B.B., the National Science Foundation (grant MCB-1158085), the Norman Hackerman Advanced Research Program (grant 010674-0034-2009), and the National Institutes of Health (grant R01 GM095538) to L.G., and the Danish Council for Independent Research - Sapere Aude, The Lundbeck Foundation and the UNIK Center for Synthetic Biology to C.J.L.s.en_US
dc.language.isoenen_US
dc.publisherROYAL SOC CHEMISTRYen_US
dc.subjectMUSCARINIC ACETYLCHOLINE-RECEPTORen_US
dc.subjectCRYSTAL-STRUCTUREen_US
dc.subjectFACIAL AMPHIPHILESen_US
dc.subjectAQUEOUS-SOLUTIONSen_US
dc.subjectCOUPLED RECEPTORen_US
dc.subjectGNG AMPHIPHILESen_US
dc.subjectSTABILIZATIONen_US
dc.subjectDETERGENTen_US
dc.subjectSOLUBILIZATIONen_US
dc.subjectCRYSTALLIZATIONen_US
dc.titleMaltose neopentyl glycol-3 (MNG-3) analogues for membrane protein studyen_US
dc.typeArticleen_US
dc.relation.no9-
dc.relation.volume140-
dc.identifier.doi10.1039/c5an00240k-
dc.relation.page3157-3163-
dc.relation.journalANALYST-
dc.contributor.googleauthorCho, Kyung Ho-
dc.contributor.googleauthorHusri, Mohd-
dc.contributor.googleauthorAmin, Anowarul-
dc.contributor.googleauthorGotfryd, Kamil-
dc.contributor.googleauthorLee, Ho Jin-
dc.contributor.googleauthorGo, Juyeon-
dc.contributor.googleauthorKim, Jin Woong-
dc.contributor.googleauthorLoland, Claus J.-
dc.contributor.googleauthorGuan, Lan-
dc.contributor.googleauthorByrne, Bernadette-
dc.contributor.googleauthorChae, Pil Seok-
dc.relation.code2015002254-
dc.sector.campusS-
dc.sector.daehakGRADUATE SCHOOL[S]-
dc.sector.departmentDEPARTMENT OF BIONANOTECHNOLOGY-
dc.identifier.pidpchae-
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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