Michael Jackson
University of Tennessee
6 Papers
129 Citations
Michael Jackson is an academic researcher from University of Tennessee. The author has contributed to research in topics: Dihydrofolate reductase & Active site. The author has an hindex of 6, co-authored 6 publications. Previous affiliations of Michael Jackson include National Institutes of Health.
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Papers
Crystal structure of a type II dihydrofolate reductase catalytic ternary complex.
TL;DR: The structure of the ternary complex provides general insights into how a mutationally challenged enzyme, i.e., an enzyme whose evolution is restricted to four-residues-at-a-time active site mutations, overcomes this fundamental limitation.
Calorimetric studies of ligand binding in R67 dihydrofolate reductase.
Michael Jackson,Shaileja Chopra,R. Derike Smiley,Patrick O'neal Maynord,Andre Rosowsky,Robert E. London,Louis A. Levy,Thomas I. Kalman,Elizabeth E. Howell +8 more
TL;DR: A role for the O4 atom of folate in a pairing preference with NADPH, which ultimately facilitates catalysis is suggested, indicating interligand pairing preferences.
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Defining the binding site of homotetrameric R67 dihydrofolate reductase and correlating binding enthalpy with catalysis.
Michael Brad Strader,Shaileja Chopra,Michael Jackson,R. Derike Smiley,Lori G. Stinnett,Jun Wu,Elizabeth E. Howell +6 more
TL;DR: Structural tightness appears to be correlated with the exothermicity of the binding interaction, this leads to the hypothesis that enthalpy-driven formation of the ternary complex in these R67 DHFR variants plays a strong role in catalysis.
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Thermodynamics and Solvent Effects on Substrate and Cofactor Binding in Escherichia coli Chromosomal Dihydrofolate Reductase
Jordan Grubbs,Sharghi Rahmanian,Alexa DeLuca,Chetan Padmashali,Michael Jackson,Michael R. Duff,Elizabeth E. Howell +6 more
TL;DR: Nonadditive enthalpy terms when binary and ternary cofactor binding events are compared suggest the presence of long-lived conformational transitions that are not included in a simple thermodynamic cycle.
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Effects of temperature and viscosity on R67 dihydrofolate reductase catalysis.
TL;DR: Surprisingly, binding of DHF, by both K(m) and K(d) determination, was found to be sensitive to added viscogens, suggesting a role for water in DHF binding.
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