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Updated: Apr 6, 2026

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection
Published on: February 18, 2014
Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol
Corey W Meadows, Gurusamy Balakrishnan1, Brandon L Kier1
1∥Department of Chemistry, University of Washington, Seattle, Washington 98195, United States.
Abstract:
Protein dynamics on the microsecond (μs) time scale were investigated by temperature-jump fluorescence spectroscopy as a function of temperature in two variants of a thermophilic alcohol dehydrogenase: W87F and W87F:H43A. Both mutants exhibit a fast, temperature-independent μs decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results, which rule out an ionizing histidine as the origin of the fluorescence quenching, are discussed in the context of a Trp49-containing dimer interface that acts as a conduit for thermally activated structural change within the protein interior.
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