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Related Experiment Videos

Atomic force microscopy of native purple membrane.

D J Müller1, J B Heymann, F Oesterhelt

  • 1M.E. Müller-Institute for Structural Biology, Biozentrum, University of Basel, Klingelkbergstr. 70, CH-4056 Basel, Switzerland. daniel.mueller@unibas.ch

Biochimica Et Biophysica Acta
|September 14, 2000
PubMed
Summary

Atomic force microscopy (AFM) reveals purple membrane (PM) surface structures and bacteriorhodopsin (BR) conformations. Loop flexibility and interactions vary with crystal packing and can be studied using AFM and force-spectroscopy.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Microscopy

Background:

  • Purple membrane (PM) contains bacteriorhodopsin (BR), a light-driven proton pump crucial for cellular energy.
  • Understanding BR structure and dynamics is key to elucidating its function.
  • AFM offers high-resolution imaging of biological surfaces in native-like conditions.

Purpose of the Study:

  • To classify major conformations of native bacteriorhodopsin (BR) surfaces in purple membrane (PM).
  • To map the variability and flexibility of polypeptide loops connecting transmembrane alpha-helices within BR.
  • To investigate the influence of crystal packing on BR loop dynamics and inter-molecular interactions.

Main Methods:

  • Atomic Force Microscopy (AFM) for subnanometer resolution imaging of PM in buffer solution.

Related Experiment Videos

  • Single molecule AFM imaging to analyze individual BR molecules and their conformations.
  • Single molecule force-spectroscopy to probe interactions between BR molecules and within secondary structure elements.

    • Main Results:

    • AFM enabled classification of major BR surface conformations and mapping of polypeptide loop variability.
    • Differences in loop position, variability, and flexibility were observed between trigonal and orthorhombic PM crystal forms.
    • Schiff base bond cleavage led to trigonal PM crystal disassembly, which was reversible upon regeneration.

    Conclusions:

    • AFM provides detailed insights into BR structure and dynamics within the PM.
    • Polypeptide loop characteristics are influenced by BR packing arrangements in the lipid bilayer.
    • Combined AFM and force-spectroscopy offer a powerful approach to study molecular interactions in biological systems.