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Related Experiment Video

Updated: May 10, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

How fast does a signal propagate through proteins?

Hui T Young¹, Scott A Edwards, Frauke Gräter

¹CAS-MPG Partner Institute and Key Laboratory for Computational Biology, Shanghai, P. R. China ; Graduate School of Chinese Academy of Sciences, Beijing, P. R. China.

|June 14, 2013

Summary

This summary is machine-generated.

Mechanical forces rapidly transmit through proteins on the picosecond scale. This study quantifies force propagation speed in alanine peptides, revealing insights into allosteric protein signaling mechanisms.

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Area of Science:

Biophysics
Molecular Biology
Computational Biology

Background:

Proteins act as molecular scaffolds for cellular signal propagation.
Understanding the speed of signal transmission through proteins is crucial for deciphering cellular mechanisms.

Purpose of the Study:

To numerically investigate the dynamics of force propagation through a single alanine peptide.
To determine the speed of mechanical signal transfer in proteins.

Main Methods:

Numerical simulations of a single alanine peptide under increased stretching forces.
Analysis of conformational and tension dynamics.

Main Results:

Force propagates along the protein backbone on the picosecond timescale.
Simulations show good agreement with coarse-grained polymer theory.
The calculated force propagation speed is approximately 50 Å/ps.

Conclusions:

The picosecond timescale of force propagation suggests rapid mechanical signaling in proteins.
The derived speed likely represents an upper limit for mechanical signal transfer in allosteric proteins and molecular machines.