139 0

Full metadata record

DC FieldValueLanguage
dc.contributor.author채필석-
dc.date.accessioned2018-03-29T07:42:39Z-
dc.date.available2018-03-29T07:42:39Z-
dc.date.issued2014-01-
dc.identifier.citationCHEMISTRY-AN ASIAN JOURNAL, JAN 2014, 9(1), p110-p116, 7p.en_US
dc.identifier.issn1861-4728-
dc.identifier.urihttp://onlinelibrary.wiley.com/doi/abs/10.1002/asia.201301097-
dc.identifier.urihttp://hdl.handle.net/20.500.11754/53810-
dc.description.abstractAmphipathic agents called detergents serve as membrane-mimetic systems to maintain the native structures of membrane proteins during their manipulation. However, membrane proteins solubilized in conventional detergents tend to undergo denaturation and aggregation, necessitating the development of novel amphipathic agents with enhanced properties. Here we describe several new amphiphiles that contain an N-oxide group as the hydrophilic portion. The new amphiphiles have been evaluated for the ability to solubilize and stabilize a fragile multi-subunit assembly from biological membranes. We found that cholate-based agents were promising in supporting retention of the native protein quaternary structure, while deoxycholate-based amphiphiles were highly efficient in extracting/solubilizing the intact superassembly from the native membrane. Monitoring superassembly solubilization and stabilization as a function of variation in amphiphile structure led us to propose that a non-hydrocarbon moiety such as an amide, ether, or a hydroxy group present in the lipophilic regions can manifest distinctive effects in the context of membrane protein manipulation.en_US
dc.description.sponsorshipThe National Research Foundation of Korea (NRF) funded by the Koreagovernment (MSIP) (grant number 2008-0061891 and2012R1A1A10 40964 to P.S.C. and S.A.) and a NIH grant (P01 GM75913to S.H.G.) supported this work. We thank Philip Laible (Argonne Na-tional Laboratory, IL, USA) for supplying membrane preparations fromR. capsulatus.en_US
dc.language.isoenen_US
dc.publisherWILEY-V C H VERLAG GMBH, BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANYen_US
dc.subjectamphiphilesen_US
dc.subjectmembrane proteinsen_US
dc.subjectmolecular designen_US
dc.subjectnon-hydrocarbon groupsen_US
dc.subjectstabilizationen_US
dc.titleHydrophobic Variations of N-Oxide Amphiphiles for Membrane Protein Manipulation: Importance of Non-hydrocarbon Groups in the Hydrophobic Portionen_US
dc.typeArticleen_US
dc.relation.no1-
dc.relation.volume9-
dc.identifier.doi10.1002/asia.201301097-
dc.relation.page110-116-
dc.relation.journalCHEMISTRY-AN ASIAN JOURNAL-
dc.contributor.googleauthorChae, Pil Seok-
dc.contributor.googleauthorSadaf, Aiman-
dc.contributor.googleauthorGellman, Samuel H.-
dc.relation.code2014027129-
dc.sector.campusS-
dc.sector.daehakGRADUATE SCHOOL[S]-
dc.sector.departmentDEPARTMENT OF BIONANOTECHNOLOGY-
dc.identifier.pidpchae-
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > ETC
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE