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dc.contributor.author채필석-
dc.date.accessioned2019-04-11T00:52:18Z-
dc.date.available2019-04-11T00:52:18Z-
dc.date.issued2016-12-
dc.identifier.citationCHEMBIOCHEM, v. 17, Issue 24, Page. 2334-2339en_US
dc.identifier.issn1439-4227-
dc.identifier.issn1439-7633-
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/full/10.1002/cbic.201600429-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/101682-
dc.description.abstractMembrane proteins encapsulated by detergent micelles are widely used for structural study. Because of their amphipathic property, detergents have the ability to maintain protein solubility and stability in an aqueous medium. However, conventional detergents have serious limitations in their scope and utility, particularly for eukaryotic membrane proteins and membrane protein complexes. Thus, a number of new agents have been devised; some have made significant contributions to membrane protein structural studies. However, few detergent design principles are available. In this study, we prepared meta and ortho isomers of the previously reported para‐substituted xylene‐linked maltoside amphiphiles (XMAs), along with alkyl chain‐length variation. The isomeric XMAs were assessed with three membrane proteins, and the meta isomer with a C12 alkyl chain was most effective at maintaining solubility/stability of the membrane proteins. We propose that interplay between the hydrophile–lipophile balance (HLB) and alkyl chain length is of central importance for high detergent efficacy. In addition, differences in inter‐alkyl‐chain distance between the isomers influence the ability of the detergents to stabilise membrane proteins.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.).en_US
dc.language.isoenen_US
dc.publisherWILEY-V C H VERLAG GMBHen_US
dc.subjectamphiphilesen_US
dc.subjectdetergentsen_US
dc.subjectmembrane proteinsen_US
dc.subjectnoncovalent interactionsen_US
dc.subjectprotein solubilizationen_US
dc.subjectprotein stabilizationen_US
dc.titleIsomeric Detergent Comparison for Membrane Protein Stability: Importance of Inter-Alkyl-Chain Distance and Alkyl Chain Lengthen_US
dc.typeArticleen_US
dc.relation.no24-
dc.relation.volume17-
dc.identifier.doi10.1002/cbic.201600429-
dc.relation.page2334-2339-
dc.relation.journalCHEMBIOCHEM-
dc.contributor.googleauthorCho, Kyung Ho-
dc.contributor.googleauthorHariharan, Parameswaran-
dc.contributor.googleauthorMortensen, Jonas S.-
dc.contributor.googleauthorDu, Yang-
dc.contributor.googleauthorNielsen, Anne K.-
dc.contributor.googleauthorByrne, Bernadette-
dc.contributor.googleauthorKobilka, Brian K.-
dc.contributor.googleauthorLoland, Claus J.-
dc.contributor.googleauthorGuan, Lan-
dc.contributor.googleauthorChae, Pil Seok-
dc.relation.code2016001508-
dc.sector.campusS-
dc.sector.daehakGRADUATE SCHOOL[S]-
dc.sector.departmentDEPARTMENT OF BIONANOTECHNOLOGY-
dc.identifier.pidpchae-
dc.identifier.orcidhttp://orcid.org/0000-0003-1799-3304-
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GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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