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Literature summary for 1.1.1.1 extracted from

  • Meadows, C.W.; Balakrishnan, G.; Kier, B.L.; Spiro, T.G.; Klinman, J.P.
    Temperature-jump fluorescence provides evidence for fully reversible microsecond dynamics in a thermophilic alcohol dehydrogenase (2015), J. Am. Chem. Soc., 137, 10060-10063.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Geobacillus stearothermophilus

Protein Variants

Protein Variants Comment Organism
W87F investigation on protein dynamics on the microsecond time scale. Mutant exhibits a fast, temperature-independent microsecond decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results rule out an ionizing histidine as the origin of the fluorescence quenching. A Trp49-containing dimer interface may act as a conduit for thermally activated structural change within the protein interior Geobacillus stearothermophilus
W87F/H43A investigation on protein dynamics on the microsecond time scale. Mutant exhibits a fast, temperature-independent microsecond decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results rule out an ionizing histidine as the origin of the fluorescence quenching. A Trp49-containing dimer interface may act as a conduit for thermally activated structural change within the protein interior Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P42328
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