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Related Experiment Video

Updated: Jul 13, 2026

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy
08:39

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Published on: December 12, 2025

Tracking single lipase molecules on a trimyristin substrate surface using quantum dots.

Andreas W Sonesson1, Ulla M Elofsson, Thomas H Callisen

  • 1YKI, Institute for Surface Chemistry, and Department of Cell Physics, Royal Institute of Technology, Stockholm, Sweden.

Langmuir : the ACS Journal of Surfaces and Colloids
|July 10, 2007
PubMed
Summary

Single lipase molecule mobility was studied using quantum dot labeling and single molecule tracking. Lipase movement showed restricted diffusion in clusters, with flow increasing distance between these active sites.

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Last Updated: Jul 13, 2026

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Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy
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Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy

Published on: February 21, 2019

Area of Science:

  • Biochemistry
  • Surface Science
  • Enzyme Kinetics

Background:

  • Understanding enzyme mobility is crucial for elucidating reaction mechanisms.
  • Lipases are key enzymes in lipid hydrolysis, with their surface interactions poorly understood.

Purpose of the Study:

  • To investigate the surface mobility and diffusion dynamics of single lipase molecules.
  • To differentiate between enzyme resting and active states on a substrate surface.

Main Methods:

  • Single molecule tracking of lipases conjugated to quantum dots.
  • Confocal laser scanning microscopy on trimyristin substrate surfaces.
  • Analysis of mean square displacement to quantify diffusion coefficients.

Main Results:

  • Lipase diffusion coefficient under no-flow conditions was (8.0+/-5.0)x10(-10) cm2/s.
  • Observed "bead on a string" trajectories with distinct "clusters" of restricted diffusion.
  • Applied flow increased the distance between clusters but did not alter diffusion within clusters.

Conclusions:

  • Lipase exhibits dual-mode behavior: active hydrolysis in clusters and flow-influenced diffusion between clusters.
  • Restricted diffusion in clusters suggests active site orientation towards the substrate.
  • The findings provide insights into enzyme-surface interactions and reaction mechanisms.