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Related Experiment Videos

Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy

F A Schabert1, C Henn, A Engel

  • 1Maurice E. Müller Institute for Microscopic Structural Biology, Universität Basel, Switzerland.

Science (New York, N.Y.)
|April 7, 1995
PubMed
Summary

Atomic force microscopy (AFM) revealed high-resolution details of porin OmpF crystals, showing protein-protein and protein-lipid interactions. This technique also detected two extracellular porin conformations, highlighting AFM

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Area of Science:

  • Structural biology
  • Biophysics
  • Materials science

Background:

  • Porins are essential membrane proteins forming channels in bacterial outer membranes.
  • Understanding porin structure and interactions is crucial for drug development and understanding cellular transport.
  • Previous crystallographic studies provided insights into porin structure.

Purpose of the Study:

  • To investigate the structural organization and interactions of two-dimensional porin OmpF crystals using atomic force microscopy (AFM).
  • To assess protein-protein and protein-lipid interactions within reconstituted porin crystals.
  • To explore the potential of AFM for monitoring conformational changes in porin structures.

Main Methods:

  • Atomic force microscopy (AFM) was employed to record topographs of porin OmpF crystals reconstituted in lipid bilayers.

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  • High lateral (10 angstroms) and vertical (1 angstrom) resolutions were achieved.
  • Crystallographic data and AFM results were integrated to analyze protein-protein interactions.
  • Lipid bilayers were modeled using kinked lipids to study protein-lipid interactions.
  • AFM was performed at specific forces (0.1 nanonewton) to probe conformational states.

    • Main Results:

    • AFM provided high-resolution structural information of porin OmpF crystals in solution.
    • Evidence for protein-protein interactions was established by combining AFM data with crystallographic findings.
    • Analysis of protein-lipid interactions was performed by modeling the lipid bilayer based on AFM contours.
    • Two distinct conformations of the extracellular porin surface were identified.
    • The study demonstrated AFM's capability to detect conformational variations.

    Conclusions:

    • AFM is a powerful tool for high-resolution structural analysis of membrane proteins like porin OmpF.
    • The study elucidated key protein-protein and protein-lipid interactions in reconstituted porin systems.
    • AFM can effectively monitor dynamic conformational changes in proteins at the molecular level.