12 0

Full metadata record

DC FieldValueLanguage
dc.contributor.author채필석-
dc.date.accessioned2019-11-25T02:42:32Z-
dc.date.available2019-11-25T02:42:32Z-
dc.date.issued2017-05-
dc.identifier.citationCHEMISTRY-A EUROPEAN JOURNAL, v. 23, no. 28, page. 6724-6729en_US
dc.identifier.issn0947-6539-
dc.identifier.issn1521-3765-
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/abs/10.1002/chem.201605016-
dc.identifier.urihttp://repository.hanyang.ac.kr/handle/20.500.11754/114021-
dc.description.abstractAs a membrane-mimetic system, detergent micelles are popularly used to extract membrane proteins from lipid environments and to maintain their solubility and stability in an aqueous medium. However, many membrane proteins encapsulated in conventional detergents tend to undergo structural degradation during extraction and purification, thus necessitating the development of new agents with enhanced properties. In the current study, two classes of new amphiphiles are introduced, resorcinarene-based glucoside and maltoside amphiphiles (designated RGAs and RMAs, respectively), for which the alkyl chains are facially segregated from the carbohydrate head groups. Of these facial amphiphiles, two RGAs (RGA-C11 and RGA-C13) conferred markedly enhanced stability to four tested membrane proteins compared to a gold-standard conventional detergent. The relatively high water solubility and micellar stability of the RGAs compared to the RMAs, along with their generally favourable behaviours for membrane protein stabilisation described here, are likely to be, at least in part, a result of the high conformational flexibility of these glucosides. This study suggests that flexibility could be an important factor in determining the suitability of new detergents for membrane protein studies.en_US
dc.description.sponsorshipThis work was supported by the National Research Foundation of Korea (NRF) funded by the Korean government (MSIP) (2016R1A2B2011257 to P.S.C., H.H., M.D. and M.E.).en_US
dc.language.isoen_USen_US
dc.publisherWILEY-V C H VERLAG GMBHen_US
dc.subjectfacial amphiphilesen_US
dc.subjectmembrane proteinsen_US
dc.subjectmolecular designen_US
dc.subjectprotein stabilityen_US
dc.subjectresorcinarene glycosidesen_US
dc.titleResorcinarene-Based Facial Glycosides: Implication of Detergent Flexibility on Membrane-Protein Stabilityen_US
dc.typeArticleen_US
dc.relation.no28-
dc.relation.volume23-
dc.identifier.doi10.1002/chem.201605016-
dc.relation.page6724-6729-
dc.relation.journalCHEMISTRY-A EUROPEAN JOURNAL-
dc.contributor.googleauthorHussain, Hazrat-
dc.contributor.googleauthorDu, Yang-
dc.contributor.googleauthorTikhonova, Elena-
dc.contributor.googleauthorMortensen, Jonas S.-
dc.contributor.googleauthorRibeiro, Orquidea-
dc.contributor.googleauthorSantillan, Claudia-
dc.contributor.googleauthorDas, Manabendra-
dc.contributor.googleauthorEhsan, Muhammad-
dc.contributor.googleauthorLoland, Claus J.-
dc.contributor.googleauthorChae, Pil Seok-
dc.relation.code2017002597-
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
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