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Proton-Coupled Dynamics in Lactose Permease
Authors:Magnus Andersson  Ana-Nicoleta Bondar  J Alfredo Freites  Douglas J Tobias  H Ronald Kaback  Stephen H White
Institution:1. Department of Physiology and Biophysics and Center for Biomembrane Systems, University of California at Irvine, Irvine, CA 92697-4560, USA;2. Department of Chemistry and Center for Biomembrane Systems, University of California at Irvine, Irvine, CA 92697-4560, USA;3. Department of Physics, Theoretical Molecular Biophysics Group, Freie Universität Berlin, Arnimallee 14, D-14195 Berlin, Germany;4. Department of Physiology and Department of Microbiology, Immunology and Molecular Genetics, Molecular Biology Institute, University of California Los Angeles, Los Angeles, CA 90095-7327, USA
Abstract:
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  • Highlights? Deprotonation of Glu325 brings H+ translocation and sugar-binding sites together ? Deprotonation of Glu325 closes the internal water-filled cytoplasmic cavity ? Deprotonated LacY inserted into DMPC lipids shows no structural rearrangements ? The structural changes show remarkable similarities to experimental observations
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