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dc.contributor.authorNavneet K. Tyagien_US
dc.contributor.authorTheeraporn Puntheeranuraken_US
dc.contributor.authorMobeen Rajaen_US
dc.contributor.authorAzad Kumaren_US
dc.contributor.authorBarbara Wimmeren_US
dc.contributor.authorIsabel Neundlingeren_US
dc.contributor.authorHermann Gruberen_US
dc.contributor.authorPeter Hinterdorferen_US
dc.contributor.authorRolf K.H. Kinneen_US
dc.contributor.otherMax Planck Institut fur molekulare Physiologieen_US
dc.contributor.otherJohannes Kepler Universitat Linzen_US
dc.contributor.otherHoward Hughes Medical Instituteen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherUniversity of Albertaen_US
dc.contributor.otherNational Institute on Agingen_US
dc.date.accessioned2018-05-03T08:05:03Z-
dc.date.available2018-05-03T08:05:03Z-
dc.date.issued2011-01-01en_US
dc.identifier.citationBiochimica et Biophysica Acta - Biomembranes. Vol.1808, No.1 (2011), 1-18en_US
dc.identifier.issn00052736en_US
dc.identifier.other2-s2.0-78649792808en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=78649792808&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/11637-
dc.description.abstractProteins mediating the transport of solutes across the cell membrane control the intracellular conditions in which life can occur. Because of the particular arrangement of spanning a lipid bilayer and the many conformations required for their function, transp ort proteins pose significant obstacles for the investigation of their structure-function relation. Crystallographic studies, if available, define the transmembrane segments in a "frozen" state and do not provide information on the dynamics of the extramembranous loops, which are similarly evolutionary conserved and thus as functionally important as the other parts of the protein. The current review presents biophysical methods that can shed light on the dynamics of transporters in the membrane. The techniques that are presented in some detail are single-molecule recognition atomic force microscopy and tryptophan scanning, which can report on the positioning of the loops and on conformational changes at the outer surface. Studies on a variety of symporters are discussed, which use gradients of sodium or protons as energy source to translocate (mainly organic) solutes against their concentration gradients into or out of the cells. Primarily, investigations of the sodium-glucose cotransporter SGLT1 are used as examples for this biophysical approach to understand transporter function. © 2010 Elsevier B.V. All rights reserved.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=78649792808&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleA biophysical glance at the outer surface of the membrane transporter SGLT1en_US
dc.typeReviewen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.bbamem.2010.07.028en_US
Appears in Collections:Scopus 2011-2015

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