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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

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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Updated: Nov 26, 2025

Monitoring Protein Adsorption with Solid-state Nanopores

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Nanopores: a versatile tool to study protein dynamics.

Sonja Schmid^1,2, Cees Dekker¹

¹Department of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, The Netherlands.

Essays in Biochemistry

|December 9, 2020

Summary

This summary is machine-generated.

Electrical nanopore sensing offers a label-free method to study protein dynamics across a wide timescale. This technique provides new insights into protein function by overcoming limitations of other single-molecule methods.

Keywords:

Conformational dynamics Nanopores Single-molecule kinetics protein dynamics protein-protein interactions

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Last Updated: Nov 26, 2025

Monitoring Protein Adsorption with Solid-state Nanopores

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Published on: December 2, 2011

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

Area of Science:

Biochemistry and Biophysics
Single-molecule biophysics
Nanotechnology applications in life sciences

Background:

Proteins are essential biomolecules driving cellular functions.
Understanding protein dynamics and conformational changes is crucial for mechanistic insights.
Existing single-molecule techniques have limitations in labeling, time bandwidth, and applicability.

Purpose of the Study:

To introduce electrical nanopore detection as a powerful tool for probing protein dynamics.
To highlight the broad timescale coverage of nanopore experiments (microseconds to hours).
To demonstrate the utility of nanopore sensing for label-free investigation of protein function.

Main Methods:

Label-free electrical nanopore detection.
Analysis of nanopore signals.
Comparison with other single-molecule techniques like FRET and force spectroscopy.

Main Results:

Nanopore experiments provide a wide time bandwidth, crucial for observing protein dynamics.
This method offers label-free detection, simplifying experimental procedures.
Nanopore sensing has successfully addressed key research questions in protein science.

Conclusions:

Electrical nanopore sensing is a versatile and accessible technique for studying protein dynamics.
It overcomes limitations of traditional single-molecule methods.
This approach enables detailed, single-molecule resolution of protein conformational changes and interactions.