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dc.contributor.author채필석-
dc.date.accessioned2017-07-28T06:25:08Z-
dc.date.available2017-07-28T06:25:08Z-
dc.date.issued2015-10-
dc.identifier.citationBIOCHEMISTRY, v. 54, NO 38, Page. 5849-5855en_US
dc.identifier.issn0006-2960-
dc.identifier.urihttp://pubs.acs.org/doi/10.1021/acs.biochem.5b00660-
dc.identifier.urihttp://hdl.handle.net/20.500.11754/28097-
dc.description.abstractThe effect of various detergents on the stability and function of the melibiose permeases of Escherichia coli (MelB(Ec)) and Salmonella typhimurium (MelB(st)) was studied. In n-dodecyl-beta-D-maltoside (DDM) or n-undecyl-beta-Dmaltoside (UDM), WT MelBst binds melibiose with an affinity similar to that in the membrane. However, with WT MelB(Ec), or MelB(st) mutants (Arg141 -˃ Cys, Arg295 -˃ Cys, or Arg363 -˃ Cys), galactoside binding is not detected in these detergents, but binding to the phosphotransferase protein IIA(Glc) is maintained. In the amphiphiles lauryl maltose neopentyl glycol (MNG-3) or glyco-diosgenin (GDN), galactoside binding with all of the MelB proteins is observed, with slightly reduced affinities. MelB(st) is more therrnostable than MelB(Ec) and the thermostability of either MelB is largely increased in MNG-3 or GDN. Therefore, the functional defect with DDM or UDM likely results from the relative instability of the sensitive MelB proteins, and stability, as well as galactoside binding, is retained in MNG-3 or GDN. Furthermore, isothermal titration calorirnetry of melibiose binding with MelB(st) shows that the favorable entropic contribution to the binding free energy is decreased in MNG-3, indicating that the conformational dynamics of MelB is restricted in this detergent.en_US
dc.description.sponsorshipThis work was supported in part by the National Science Foundation, Directorate for Biological Sciences (grant MCB-1158085 to L.G.); by the U.S. Department of Health and Human Services, National Institutes of Health (grant R01 GM095538 to L.G.); and by the Korean government (MSIP), the National Research Foundation of Korea (grant 2013R1A2A2A03067623 to P.S.C.).en_US
dc.language.isoenen_US
dc.publisherAMER CHEMICAL SOCen_US
dc.subjectRESONANCE ENERGY-TRANSFERen_US
dc.subjectSEROVAR TYPHIMURIUM MELBen_US
dc.subjectESCHERICHIA-COLIen_US
dc.subjectLACTOSE PERMEASEen_US
dc.subjectTRANSPORT PROTEINSen_US
dc.subjectMEMBRANE-VESICLESen_US
dc.subjectNA+en_US
dc.subjectSTABILIZATIONen_US
dc.subjectAMPHIPHILESen_US
dc.subjectMECHANISMen_US
dc.titleEffect of Detergents on Galactoside Binding by Melibiose Permeasesen_US
dc.typeArticleen_US
dc.relation.no38-
dc.relation.volume54-
dc.identifier.doi10.1021/acs.biochem.5b00660-
dc.relation.page5849-5855-
dc.relation.journalBIOCHEMISTRY-
dc.contributor.googleauthorAmin, Anowarul-
dc.contributor.googleauthorHariharan, Parameswaran-
dc.contributor.googleauthorChae, Pil Seok-
dc.contributor.googleauthorGuan, Lan-
dc.relation.code2015000442-
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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