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Water permeation across biological membranes: Mechanism and dynamics of Aquaporin-1 and GlpF.

MPG-Autoren
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de Groot,  B. L.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Grubmueller,  H.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

Externe Ressourcen

http://www.sciencemag.org/content/294/5550/2353.full.pdf
(Verlagsversion)

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599912.pdf
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Zitation

de Groot, B. L., & Grubmueller, H. (2001). Water permeation across biological membranes: Mechanism and dynamics of Aquaporin-1 and GlpF. Science, 294, 2353-2357.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0012-F5D8-7
Zusammenfassung
Real time” molecular dynamics simulations of water permeation through human aquaporin-1 (AQP1) and the bacterial glycerol facilitator GlpF are presented. We obtained time-resolved, atomic-resolution models of the permeation mechanism across these highly selective membrane channels. Both proteins act as two-stage filters: Conserved fingerprint [asparagine-proline-alanine (NPA)] motifs form a selectivity-determining region; a second (aromatic/arginine) region is proposed to function as a proton filter. Hydrophobic regions near the NPA motifs are rate-limiting water barriers. In AQP1, a fine-tuned water dipole rotation during passage is essential for water selectivity. In GlpF, a glycerol-mediated “induced fit” gating motion is proposed to generate selectivity for glycerol over water.