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000698132 019__ $$a879864891
000698132 020__ $$a9783642538391$$qelectronic book
000698132 020__ $$a3642538398$$qelectronic book
000698132 020__ $$z9783642538384
000698132 0247_ $$a10.1007/978-3-642-53839-1$$2doi
000698132 035__ $$aSP(OCoLC)ocn875003166
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000698132 24500 $$aMembrane transport mechanism$$h[electronic resource] :$$b3D structure and beyond /$$cReinhard Krämer, Christine Ziegler, editors.
000698132 264_1 $$aHeidelberg :$$bSpringer,$$c2014.
000698132 300__ $$a1 online resource (xii, 272 pages) :$$billustrations (some color).
000698132 336__ $$atext$$btxt$$2rdacontent
000698132 337__ $$acomputer$$bc$$2rdamedia
000698132 338__ $$aonline resource$$bcr$$2rdacarrier
000698132 4901_ $$aSpringer Series in Biophysics,$$x0932-2353 ;$$v17
000698132 5050_ $$aDance Lessons for Proteins: The Dynamics and Thermodynamics of a Sodium/Aspartate Symporter -- Characterizing the Structure, Function and Evolution of Human Solute Carrier (SLC) Transporters Using Computational Approaches -- Structures of the Prokaryotic Galactose Transporter vSGLT and Their Implications on Alternating Access Mechanism in Human SGLT1 -- Moving Crystallographic Snapshots: A Mechanism for Transport Regulation in BetP -- Development of Refined Homology Models: Adding the Missing Information to the Medically Relevant Neurotransmitter Transporters -- The Life and Times of Lac Permease: Crystals Ain't Enough -- Alternating Access Within the POT Family of Oligopeptide -- Proton Symporters -- The Maltose ABC Transporter: Where Structure Meets Function -- Cooperative Transport Mechanism and Proton-Coupling in the Multidrug Efflux Transporter Complex ArcAB-TolC -- What Can a Living Fossil Tell Us About Evolution and Mechanism of Ion-Coupled Transporters: The Story of Small Multidrug Transporters Symmetrically Asymmetric: EmrE Seen from the NMR Perspective.
000698132 506__ $$aAccess limited to authorized users.
000698132 520__ $$aThis book provides a molecular view of membrane transport by means of numerous biochemical and biophysical techniques. The rapidly growing number of atomic structures of transporters in different conformations and the constant progress in bioinformatics have recently added deeper insights. The unifying mechanism of energized solute transport across membranes is assumed to consist of the conformational cycling of a carrier protein to provide access to substrate binding sites from either side of a cellular membrane. Due to the central role of active membrane transport there is considerable interest in deciphering the principles of one of the most fundamental processes in nature: the alternating access mechanism. This book brings together particularly significant structure-function studies on a variety of carrier systems from different transporter families: Glutamate symporters, LeuT-like fold transporters, MFS transporters and SMR (RND) exporters, as well as ABC-type importers. The selected examples impressively demonstrate how the combination of functional analysis, crystallography, investigation of dynamics and computational studies has made it possible to create a conclusive picture, or, more precisely, a molecular movie. Although we are still far from a complete molecular description of the alternating access mechanism, remarkable progress has been made from static snapshots towards membrane transport dynamics.
000698132 588__ $$aDescription based on online resource; title from PDF title page (SpringerLink, viewed March 17, 2014).
000698132 650_0 $$aBiological transport.
000698132 7001_ $$aKramer, Reinhard,$$eeditor of compilation.
000698132 7001_ $$aZiegler, Christine,$$eeditor of compilation.
000698132 830_0 $$aSpringer series in biophysics ;$$vv. 17.
000698132 85280 $$bebk$$hSpringerLink
000698132 85640 $$3SpringerLink$$uhttps://univsouthin.idm.oclc.org/login?url=http://dx.doi.org/10.1007/978-3-642-53839-1$$zOnline Access
000698132 909CO $$ooai:library.usi.edu:698132$$pGLOBAL_SET
000698132 980__ $$aEBOOK
000698132 980__ $$aBIB
000698132 982__ $$aEbook
000698132 983__ $$aOnline