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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 Location

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4970856/
No data is associated with this publication.
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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