Mike Connolly

My research is on the use of computer simulations to study the role that protein dynamics play in enzyme catalysis. Recently it has been proposed that the heat capacity of activation of an enzyme-catalysed reaction is “tuned” to the optimum temperature of enzymes, and also accounts for the curvature of enzyme rate profiles[1-2]. This unique view could provide an explanation as to why enzymes are such large proteins, why they have such complex and varied structures, and how the optimum temperature of each enzyme is “tuned” by evolution. My work focuses on measuring thermodynamic properties of enzyme-catalyzed reactions using classical molecular dynamics (MD) simulations, and other computational chemistry techniques, to investigate the physical origins of enzyme catalysis, and to examine the role of protein dynamics in enzyme function.


Previous work:

Before coming to Bristol I completed an MChem at the University of Oxford where I completed an experimental and computational masters project studying Zintl ions with the Goicoechea and McGrady groups. I then joined the TMCS CDT, where I gained an MSc in Theoretical and Computational Chemistry, which included a short research project at the University of Southampton working with Professor Syma Khalid on simulating an antimicrobial with a model bacteria membrane, using coarse-grained and atomistic molecular dynamics. I then joined the Mulholland group to begin working on my PhD project.



  1. Arcus, V. L.; Prentice, E. J.; Hobbs, J. K.; Mulholland, A. J.; Van der Kamp, M. W.; Pudney, C. R.; Parker, E. J.; Schipper, L. A. On the Temperature Dependence of Enzyme-Catalyzed Rates. Biochemistry (Mosc.) 2016, 55 (12), 1681–1688 DOI: 10.1021/acs.biochem.5b01094.
  2. Hobbs, J. K.; Jiao, W.; Easter, A. D.; Parker, E. J.; Schipper, L. A.; Arcus, V. L. Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates. ACS Chem. Biol. 2013, 8 (11), 2388–2393 DOI: 10.1021/cb4005029.
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