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Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy

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  • L Schmüser
  • M Trefz, University Medical Centre Mainz, Mainz, Germany
  • ,
  • S J Roeters, University of Amsterdam
  • ,
  • W Beckner, University of Washington
  • ,
  • J Pfaendtner, University of Washington
  • ,
  • D Otzen
  • S Woutersen, University of Amsterdam
  • ,
  • M Bonn, Max Planck Institute for Polymer Research
  • ,
  • D Schneider, University of Mainz
  • ,
  • T Weidner

High-resolution structural information on membrane proteins is essential for understanding cell biology and for the structure-based design of new medical drugs and drug delivery strategies. X-ray diffraction (XRD) can provide angstrom-level information about the structure of membrane proteins, yet for XRD experiments, proteins are removed from their native membrane environment, chemically stabilized, and crystallized, all of which can compromise the conformation. Here, we describe how a combination of surface-sensitive vibrational spectroscopy and molecular dynamics simulations can account for the native membrane environment. We observe the structure of a glycerol facilitator channel (GlpF), an aquaporin membrane channel finely tuned to selectively transport water and glycerol molecules across the membrane barrier. We find subtle but significant differences between the XRD structure and the inferred in situ structure of GlpF.

TidsskriftLangmuir : the ACS journal of surfaces and colloids
Sider (fra-til)13452-13459
Antal sider8
StatusUdgivet - nov. 2021

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