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Related Experiment Video

Updated: Jul 4, 2026

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection

Published on: February 18, 2014

WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy.

David Spetzler¹, Justin York, James Martin

¹School of Life Sciences, Arizona State University, P.O. Box 874501, Tempe, AZ 85287-4501, USA.

Methods (San Diego, Calif.)

|June 21, 2008

Summary

Researchers developed a new technique to track molecular motor rotation at ultra-high speeds. This method precisely measures the angular changes in the F(1)-ATPase gamma-subunit, revealing its transition times.

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Last Updated: Jul 4, 2026

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Published on: May 30, 2021

Area of Science:

Biophysics
Molecular Biology
Nanotechnology

Background:

Molecular motors are essential biological machines.
Understanding their conformational changes is key to deciphering their function.
Previous methods lacked the required temporal resolution.

Purpose of the Study:

To develop a novel, high-time-resolution method for detecting angular conformational changes in molecular motors.
To measure the velocity and transition times of the F(1)-ATPase gamma-subunit.

Main Methods:

Utilized a gold nanorod attached to the gamma-subunit of immobilized F(1)-ATPase.
Measured variations in scattered light intensity to track angular position.
Achieved a time resolution of 2.5 microseconds (400,000 frames per second).

Main Results:

Demonstrated a novel method capable of detecting subtle angular conformational changes.
Achieved unprecedented acquisition rates for high-speed molecular dynamics.
Successfully resolved the velocity of the F(1)-ATPase gamma-subunit during conformational transitions.

Conclusions:

The developed method offers high sensitivity and temporal resolution for studying molecular motors.
This technique enables detailed analysis of rotary dynamics in biological systems.
Provides new insights into the mechanics of enzymes like F(1)-ATPase.