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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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Observing Single-Molecule Dynamics at Millimolar Concentrations.

Marcel P Goldschen-Ohm1, David S White1,2, Vadim A Klenchin1

  • 1Department of Neuroscience, University of Wisconsin-Madison, 1111 Highland Ave., Madison, WI, 53705, USA.

Angewandte Chemie (International Ed. in English)
|January 25, 2017
PubMed
Summary
This summary is machine-generated.

We developed a new method combining nanophotonic zero-mode waveguides (ZMWs) and fluorescence resonance energy transfer (FRET) to study molecular interactions at high concentrations. This breakthrough enables single-molecule analysis of previously inaccessible biological targets.

Keywords:
FRETkineticsnucleotidessingle-molecule studieszero-mode waveguide

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Area of Science:

  • Biophysics
  • Chemical Kinetics
  • Nanotechnology

Background:

  • Single-molecule fluorescence microscopy offers insights into chemical dynamics and molecular interactions.
  • Current limitations include low concentrations of fluorescent species and suitability only for high-affinity reactions.

Purpose of the Study:

  • To develop a method enabling single-molecule analysis of molecular association dynamics at millimolar concentrations.
  • To expand the applicability of single-molecule techniques to a broader range of molecular targets and biological processes.

Main Methods:

  • Integration of nanophotonic zero-mode waveguides (ZMWs) with fluorescence resonance energy transfer (FRET).
  • Enabling observation of single-molecule dynamics at concentrations over 100-fold higher than previously possible.

Main Results:

  • Demonstrated successful single-molecule association dynamics measurement at millimolar concentrations.
  • Revealed that cGMP binding to pacemaking ion channels is hindered by a slow internal conformational change.

Conclusions:

  • The combined ZMW-FRET approach significantly enhances the concentration range for single-molecule studies.
  • This technique opens new avenues for investigating molecular interactions in biologically and chemically relevant conditions.