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dc.contributor.author채필석-
dc.date.accessioned2018-03-13T09:51:08Z-
dc.date.available2018-03-13T09:51:08Z-
dc.date.issued2013-11-
dc.identifier.citationCHEMISTRY-A EUROPEAN JOURNAL, 권: 19, 호: 46, 페이지: 15645-15651en_US
dc.identifier.issn0947-6539-
dc.identifier.issn1521-3765-
dc.identifier.urihttp://onlinelibrary.wiley.com/doi/10.1002/chem.201301423/abstract-
dc.identifier.urihttp://hdl.handle.net/20.500.11754/46325-
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.en_US
dc.description.sponsorshipThis work was supported by the National Research Foundation of Korea (NRF) funded by the Korea government (MSIP) (grant number 2008-0061891 and 2012R1A1A1040964 to P. S. C., K. H. C., H. E. B.), NIHgrant P01 GM75913 (S. H. G.), NS28471 (B. K.), the European Community's Seventh Framework Programme FP7/2007-2013 under grant agreement number HEALTH-F4-2007-201924, EDICT Consortium (B. B., K. G., U. G.), the Danish National Research Council (C.J.L., U. G.), the Lundbeck Foundation (S. G. F. R., C.J.L., U. G.), and NIH grants R01 GM95538 and R21 HL087895 (to L. G.). R. R. was funded by the Defence, Science and Technology Laboratories (DSTL), Porton Down, UK. We thank Philip Laible (Argonne National Laboratory) and Elodie Point and Jean-Luc Popot (Universite Paris-7) for supplying membrane preparations from R. capsulatus and purple membrane, respectively. We also thank Chiara Lee and David Drew (Imperial College London) and Jonathan Ruprecht (Medical Research Council-Mitochondrial Biology Unit, Cambridge) and Gary Cecchini (University of California, San Francisco) for providing purified GlpG and SQR samples, respectively. We also thank Shalika Nurva for her technical assistance in the MelB assay.en_US
dc.language.isoenen_US
dc.publisherWILEY-V C H VERLAG GMBHen_US
dc.subjectamphiphilesen_US
dc.subjectmembrane proteinsen_US
dc.subjectmolecular designen_US
dc.subjectprotein structures; stabilizationen_US
dc.titleNovel Tripod Amphiphiles for Membrane Protein Analysisen_US
dc.typeArticleen_US
dc.relation.no46-
dc.relation.volume19-
dc.identifier.doi10.1002/chem.201301423-
dc.relation.page15645-15651-
dc.relation.journalCHEMISTRY-A EUROPEAN JOURNAL-
dc.contributor.googleauthorChae, Pil Seok-
dc.contributor.googleauthorKruse, Andrew C.-
dc.contributor.googleauthorGotfryd, Kamil-
dc.contributor.googleauthorRana, Rohini R.-
dc.contributor.googleauthorCho, Kyung Ho-
dc.contributor.googleauthorRasmussen, Soren G. F.-
dc.contributor.googleauthorBae, Hyoung Eun-
dc.contributor.googleauthorChandra, Richa-
dc.contributor.googleauthorGether, Ulrik-
dc.contributor.googleauthorGuan, Lan-
dc.relation.code2013009401-
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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