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Related Experiment Videos

Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope:

D J Müller1, C A Schoenenberger, F Schabert

  • 1Biozentrum, M.E. Müller Institute for Microscopy, Basel, Switzerland.

Journal of Structural Biology
|July 1, 1997
PubMed
Summary

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Atomic force microscopy revealed dynamic structural changes in membrane proteins like OmpF porin and bacteriorhodopsin under physiological conditions. This technique allows for the direct observation of function-related conformational changes in biomolecules.

Area of Science:

  • Biophysics
  • Structural Biology
  • Microscopy

Background:

  • Membrane proteins play crucial roles in cellular functions.
  • Understanding their dynamic structural changes is key to elucidating their mechanisms of action.
  • Atomic Force Microscopy (AFM) offers high-resolution imaging capabilities for biological samples.

Purpose of the Study:

  • To investigate the structural dynamics of three distinct membrane proteins using AFM.
  • To determine if AFM can resolve function-related conformational changes in biomolecules under physiological conditions.
  • To explore the potential of AFM in studying protein behavior in buffer solutions.

Main Methods:

  • High-resolution Atomic Force Microscopy (AFM) was employed.
  • Investigations were conducted on OmpF porin (Escherichia coli), bacteriorhodopsin (Halobacterium salinarium), and the HPI layer (Deinoccocus radiodurans).

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  • Experiments were performed in buffer solution, simulating physiological conditions, with force variations applied to the scanning stylus.

    • Main Results:

    • AFM achieved a resolution of up to 0.8 nm, enabling detection of subtle structural differences.
    • OmpF porin displayed distinct static conformations, potentially linked to ion channel conductivity states.
    • Reversible structural transformations were observed in bacteriorhodopsin trimers upon force reduction (300 to 100 pN).
    • Individual pores within the HPI layer exhibited reversible switching between 'open' and 'closed' states.

    Conclusions:

    • AFM is a feasible technique for the direct observation of function-related conformational changes in biomolecules.
    • The study demonstrates that AFM can resolve dynamic structural alterations in membrane proteins under near-physiological conditions.
    • These findings open avenues for detailed structural and functional studies of membrane proteins using AFM.