Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol Dehydrogenase.
- Author(s): Meadows, Corey W
- Balakrishnan, Gurusamy
- Kier, Brandon L
- Spiro, Thomas G
- Klinman, Judith P
- et al.
Published Web Locationhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4970856/
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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