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

L Schmüser, M Trefz, S J Roeters, W Beckner, J Pfaendtner, D Otzen, S Woutersen, M Bonn, D Schneider, T Weidner

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Abstract

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.

Original languageEnglish
JournalLangmuir : the ACS journal of surfaces and colloids
Volume37
Issue45
Pages (from-to)13452-13459
Number of pages8
ISSN0743-7463
DOIs
Publication statusPublished - Nov 2021

Keywords

  • BILAYER
  • CHANNEL
  • CRYSTAL
  • GLYCEROL
  • INTERFACE
  • MOLECULAR-DYNAMICS
  • ORIENTATION
  • PEPTIDE
  • PROTEIN
  • VIBRATIONAL SPECTROSCOPY

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