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Related Experiment Video

Updated: Feb 8, 2026

Monitoring Protein Adsorption with Solid-state Nanopores

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Uncovering Hidden Protein Conformations with High Bandwidth Nanopore Measurements.

Kyril Kavetsky^1,2, Sabine Hong¹, Chih-Yuan Lin¹

¹Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.

|February 6, 2026

Summary

This summary is machine-generated.

Advanced nanopore measurements revealed six distinct folding states for the heme protein cytochrome c. This technique provides high-resolution insights into protein dynamics and conformational changes during translocation.

Keywords:

Nanopore high bandwidth low noise amplifier protein folding single molecule ultrafast protein translocation

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Area of Science:

Molecular Biophysics
Nanotechnology
Biochemistry

Background:

Nanopore technology offers high spatial and temporal resolution for molecular structural probing.
Understanding protein folding dynamics is crucial in molecular biology and disease research.

Purpose of the Study:

To investigate the multistate folding of the heme protein cytochrome c using advanced nanopore measurements.
To characterize protein states and transitions during translocation through a nanopore.

Main Methods:

Utilized high signal-to-noise, 1-10 MHz bandwidth translocation measurements.
Employed optimally designed silicon nitride nanopores (2.3-3.3 nm diameter) with a denaturant (Gdm-Cl).
Applied an electric field of ~250 kV/cm for protein probing.

Main Results:

Identified six distinct protein states based on current blockade levels using Bayesian Information Criterion analysis.
Calculated transition probabilities between identified protein states.
Determined conditional probabilities of protein exiting the pore from each state.

Conclusions:

The study successfully characterized the multistate folding of cytochrome c using nanopore sensing.
The findings validate the nanopore method for detailed analysis of protein conformational dynamics.
Simulated events confirmed the experimental model and data interpretation.