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GFP's mechanical intermediate states.

John Saeger1, Vesa P Hytönen, Enrico Klotzsch

  • 1Laboratory of Applied Mechanobiology, Department of Health Sciences and Technology, ETH Zürich, Zürich, Switzerland.

Plos One
|November 3, 2012
PubMed
Summary
This summary is machine-generated.

Green fluorescent protein (GFP) fluorescence dims when mechanically stretched due to N-terminal helix loss. This structural change affects protonation, potentially switching off GFP

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Green fluorescent protein (GFP) is a vital tool in life sciences, widely used as a fluorescence marker.
  • GFP's utility is expanding to probe mechanical force and strain, but its response to stretching is not well understood.

Purpose of the Study:

  • To investigate how mechanical stretching affects GFP fluorescence.
  • To derive high-resolution structural models of intermediate states during GFP stretching.
  • To create and analyze GFP mutants mimicking these mechanical states.

Main Methods:

  • Steered molecular dynamics (SMD) simulations to model mechanical intermediates of stretched GFP.
  • Creation of EGFP and EYFP mutants based on simulated structural models.
  • Spectroscopic analysis of mutant fluorescence properties.

Main Results:

  • A population of EGFP mutants lacking the N-terminal α-helix showed significantly reduced fluorescence.
  • The fluorescence lifetime associated with the anionic chromophore state was unaffected by the N-terminal deletion.
  • Structural changes in GFP upon stretching influence chromophore protonation state.

Conclusions:

  • N-terminal deletions in GFP can alter chromophore protonation, leading to fluorescence quenching.
  • This provides a mechanism for how mechanical forces can modulate GFP fluorescence.
  • Understanding these mechanical responses is crucial for developing advanced GFP-based biosensors.