Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Phase Transitions: Melting and Freezing

Phase Transitions: Melting and Freezing

Heating a crystalline solid increases the average energy of its atoms, molecules, or ions, and the solid gets hotter. At some point, the added energy becomes large enough to partially overcome the forces holding the molecules or ions of the solid in their fixed positions, and the solid begins the process of transitioning to the liquid state or melting. At this point, the temperature of the solid stops rising, despite the continual input of heat, and it remains constant until all of the solid is...

Mechanical Protein Functions

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Rhodanese-enabled signal conversion and nanoporous gold electrotransduction for dual sensing of cyanide and sulfite in environmental waters.

Biosensors & bioelectronics·2026

Same author

A labile sulfur ligand in a three-cysteine-coordinated [2Fe-2S] cluster mediates sulfide sensing in NreB.

Nature communications·2026

Same author

High-Performance SiPM Detection Module for Ultra-Fast Time-Resolved Measurements.

Sensors (Basel, Switzerland)·2026

Same author

Zero-valent sulfur is the product of assimilatory sulfite reductase and a substrate of cysteine synthase.

Applied and environmental microbiology·2026

Same author

Power-dependent single-molecule dynamics of dark quencher blinking in QSY9/Cy3B: Diffusion-binding experiment and theory.

The Journal of chemical physics·2026

Same author

An ArsR-type transcriptional regulator, SoxR, regulates sulfur oxidization (Sox) system in Cupriavidus pinatubonensis JMP134.

BMC microbiology·2026

Search research articles

Related Experiment Video

Updated: Jul 1, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Protein conformational dynamics probed by single-molecule electron transfer.

Haw Yang¹, Guobin Luo, Pallop Karnchanaphanurach

¹Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.

Science (New York, N.Y.)

|October 11, 2003

Summary

This summary is machine-generated.

Researchers used electron transfer in single protein molecules to observe angstrom-scale structural changes. This revealed protein conformational fluctuations linked to catalytic reactivity.

More Related Videos

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Related Experiment Videos

Last Updated: Jul 1, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Area of Science:

Biophysics
Protein dynamics
Electron transfer

Background:

Electron transfer serves as a sensitive probe for angstrom-scale structural dynamics in single protein molecules.
Flavin reductases utilize flavin and tyrosine residues where photo-induced electron transfer can occur.

Purpose of the Study:

To investigate angstrom-scale structural changes in single protein molecules using electron transfer as a probe.
To correlate protein conformational fluctuations with catalytic reactivity.

Main Methods:

Utilized single-molecule fluorescence lifetime measurements of flavin.
Employed photo-induced electron transfer between flavin and tyrosine as a distance probe.
Performed correlation analysis on observed distance variations.

Main Results:

Observed variations in flavin-tyrosine distance over time at the single-molecule level.
Determined the potential of mean force between flavin and tyrosine.
Revealed conformational fluctuations across multiple timescales (microseconds to seconds).

Conclusions:

Single-molecule electron transfer can resolve angstrom-scale protein structural dynamics.
Protein conformational fluctuations are linked to changes in catalytic reactivity.
The existence of multiple interconverting conformers influences enzyme function.