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Related Experiment Video

Updated: Feb 12, 2026

Monitoring Protein Adsorption with Solid-state Nanopores

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Differential Enzyme Flexibility Probed Using Solid-State Nanopores.

Rui Hu^1,2, João V Rodrigues³, Pradeep Waduge⁴

¹State Key Laboratory for Mesoscopic Physics and Electron Microscopy Laboratory, School of Physics , Peking University , Beijing 100871 , People's Republic of China.

|April 10, 2018

Summary

This summary is machine-generated.

Measuring subtle protein flexibility changes is crucial for understanding function and disease. This study shows nanopore electrical signatures reliably detect conformational dynamics in single protein molecules, advancing biophysical analysis.

Keywords:

DHFR adenylate kinase bis-ANS protein flexibility solid-state nanopore

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Area of Science:

Biophysics
Molecular Biology
Nanotechnology

Background:

Protein function relies on dynamic conformational changes and flexibility.
Measuring these subtle changes in active vs. resting states is vital for therapeutic development but technically challenging.
Previous work showed electrical signatures of proteins in nanopores correlate with conformational dynamics.

Purpose of the Study:

To resolve subtle flexibility variations in dihydrofolate reductase (DHFR) mutants using unlabeled single molecules.
To establish nanopore measurements as a reliable method for probing protein conformational diversity.
To optimize experimental conditions for detecting protein dynamics via nanopore sensing.

Main Methods:

Utilized solid-state nanopore sensing to measure electrical signatures of single protein molecules in solution.
Investigated adenylate kinase to validate size and flexibility changes upon ligand binding.
Optimized voltage bias and pore geometry for protein transport analysis.
Systematically studied wild-type and mutant DHFR proteins.

Main Results:

Demonstrated that nanopore electrical signal amplitude breadth correlates with protein conformational dynamics.
Observed distinct electrical signatures corresponding to different protein conformations (e.g., closed state of adenylate kinase).
Found good correlation between nanopore-measured dynamics and bulk fluorescence probe measurements for DHFR.

Conclusions:

Nanopore-based electrical measurements reliably detect and quantify conformational diversity in native protein ensembles.
This technique offers a sensitive approach to study protein dynamics, crucial for understanding function and disease.
The findings pave the way for advanced biophysical characterization of proteins at the single-molecule level.