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@ARTICLE{Dreyer:201207,
      author       = {Dreyer, Jens and Zhang, Chao and Ippoliti, Emiliano and
                      Carloni, Paolo},
      title        = {{R}ole of the {M}embrane {D}ipole {P}otential for {P}roton
                      {T}ransport in {G}ramicidin {A} {E}mbedded in a {DMPC}
                      {B}ilayer},
      journal      = {Journal of chemical theory and computation},
      volume       = {9},
      number       = {8},
      issn         = {1549-9626},
      address      = {Washington, DC},
      publisher    = {American Chemical Society (ACS)},
      reportid     = {FZJ-2015-03512},
      pages        = {3826 - 3831},
      year         = {2013},
      abstract     = {The membrane potential at the water/phospholipid interfaces
                      may play a key role for proton conduction of gramicidin A
                      (gA). Here we address this issue by Density Functional
                      Theory-based molecular dynamics and metadynamics
                      simulations. The calculations, performed on gA embedded in a
                      solvated 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)
                      model membrane environment (about 2,000 atoms), indicate
                      that (i) the membrane dipole potential rises at the channel
                      mouth by ∼0.4 V. A similar value has been measured for gA
                      embedded in a DMPC monolayer; (ii) the calculated free
                      energy barrier is located at the channel entrance,
                      consistent with experiments comparing gA proton conduction
                      in different bilayers. The electronic structures of the
                      proton ligands (water molecules and peptide units) are
                      similar to those in the bulk solvent. Based on these
                      results, we suggest an important role of the membrane dipole
                      potential for the free energy barrier of proton permeation
                      of gA. This may provide a rationale for the large increase
                      in the rate of proton conduction under application of a
                      transmembrane voltage, as observed experimentally. Our
                      calculations might suggest also a role for proton
                      desolvation for the permeation process. This role has
                      already emerged from EVB calculations on gA embedded in a
                      model membrane.},
      cin          = {GRS / IAS-5},
      ddc          = {540},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000323193500054},
      doi          = {10.1021/ct400374n},
      url          = {https://juser.fz-juelich.de/record/201207},
}