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Updated: Jul 4, 2026

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WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy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.
Abstract:
We report a novel method to detect angular conformational changes of a molecular motor in a manner sensitive enough to achieve acquisition rates with a time resolution of 2.5mus (equivalent to 400,000fps). We show that this method has sufficient sensitivity to resolve the velocity of the F(1)-ATPase gamma-subunit as it travels from one conformational state to another (transition time). Rotation is detected via a gold nanorod attached to the rotating gamma-subunit of an immobilized F(1)-ATPase. Variations in scattered light intensity allow precise measurement of changes in angular position of the rod below the diffraction limit of light.
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