• openAccess   Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase 

      Luk, Louis Y. P.; Ruiz-Pernía, José Javier; Adesina, Aduragbemi S.; Loveridge, E. Joel; Tuñón, Iñaki; Moliner, Vicent; Allemann, Rudolf K. Wiley (2015-07-27)
      Experimental and computational approaches have long been employed to define the role of protein motions in en- zyme catalysis, but a refined experimental method for locating the origin of dynamic effects has not previously ...
    • openAccess   Increased Dynamic Effects in a Catalytically Compromised Variant of Escherichia coli Dihydrofolate Reductase 

      Ruiz-Pernía, José Javier; Luk, Louis Y. P.; García Meseguer, Rafael; Martí Forés, Sergio; Loveridge, E. Joel; Tuñón, Iñaki; Moliner, Vicent; Allemann, Rudolf K. American Chemical Society (2013)
      Isotopic substitution (15N, 13C, 2H) of a catalytically compromised variant of Escherichia coli dihydrofolate reductase, EcDHFR-N23PP/S148A, has been used to investigate the effect of these mutations on catalysis. The ...
    • openAccess   Minimization of dynamic effects in the evolution of dihydrofolate reductase 

      Ruiz-Pernía, José Javier; Behiry, Enas; Luk, Louis Y. P.; Loveridge, E. Joel; Tuñón, Iñaki; Moliner, Vicent; Allemann, Rudolf K. Royal Society of Chemistry (2016)
      Protein isotope labeling is a powerful technique to probe functionally important motions in enzyme catalysis and can be applied to investigate the conformational dynamics of proteins. Previous investigations have indicated ...
    • openAccess   Protein Isotope Effects in Dihydrofolate Reductase From Geobacillus stearothermophilus Show Entropic–Enthalpic Compensatory Effects on the Rate Constant 

      Luk, Louis Y. P.; Ruiz-Pernía, José Javier; Dawson, William M.; Loveridge, E. Joel; Tuñón, Iñaki; Moliner, Vicent; Allemann, Rudolf K. American Chemical Society (2014)
      Catalysis by dihydrofolate reductase from the moderately thermophilic bacterium Geobacillus stearothermophilus (BsDHFR) was investigated by isotope substitution of the enzyme. The enzyme kinetic isotope effect for hydride ...
    • closedAccess   Unraveling the role of protein dynamics in dihydrofolate reductase catalysis 

      Moliner, Vicent; Ruiz-Pernía, José Javier; Luk, Louis Y. P.; Dawson, William M.; Roca, Maite; Loveridge, E. Joel; Glowacki, David R.; Harvey, Jeremy N.; Mulholland, Adrian J.; Tuñón, Iñaki; Allemann, Rudolf K. National Academy of Sciences (2013)
      Protein dynamics have controversially been proposed to be at the heart of enzyme catalysis, but identification and analysis of dynamical effects in enzyme-catalyzed reactions have proved very challenging. Here, we tackle ...