6533b854fe1ef96bd12af3a2
RESEARCH PRODUCT
Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy
Daniel E. OtzenTobias WeidnerTobias WeidnerM. TrefzSander WoutersenWesley BecknerLars SchmüserSteven J. RoetersJim PfaendtnerDirk SchneiderMischa Bonnsubject
GlycerolInfrared spectroscopyAquaporinPROTEINAquaporinsVIBRATIONAL SPECTROSCOPYMolecular dynamicsCHANNELElectrochemistryGeneral Materials SciencePEPTIDESpectroscopyCRYSTALChemistryEscherichia coli ProteinsSpectrum AnalysisMembrane structureWaterSurfaces and InterfacesCondensed Matter PhysicsBILAYERGLYCEROLINTERFACEMembraneMembrane proteinMOLECULAR-DYNAMICSBiophysicsMembrane channelORIENTATIONSum frequency generation spectroscopydescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2021-11-16 |