Author

V. L. Arcus

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Approach:statistical model· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:development & morphogenesis· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

A. J. Mulholland· 3 shared M. W. van der Kamp· 3 shared E. J. Prentice· 2 shared K. L. Kraakman· 2 shared A. K. Warrender· 1 shared A. Steyn-Ross· 1 shared C. J. Hamill· 1 shared C. R. Pudney· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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3 shared papersBiochemistry

A. J. Mulholland

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Author profile →

3 papers

Recent·Most cited

Cooperative conformational transitions and the temperature dependence of enzyme catalysis

E. J. Walker, C. J. Hamill, R. M. Crean, M. S. Connolly, A. K. Warrender, K. L. Kraakman, E. J. Prentice, A. Steyn-Ross, M. Steyn-Ross, C. R. Pudney, M. W. van der Kamp, L. A. Schipper, A. J. Mulholland, V. L. Arcus

This study investigates the temperature dependence of enzyme catalysis by analyzing MalL and its mutants, showing cooperative conformational transitions and introducing models to explain non-Arrhenius behavior.

bioRxiv · Jul 6, 2023 · PreprintBiochemistry

Evolution of dynamical networks enhances catalysis in a designer enzyme

H. A. Bunzel, R. Anderson, D. Hilvert, V. L. Arcus, M. W. van der Kamp, A. J. Mulholland

This study shows that directed evolution of a designer enzyme introduces dynamical changes that increase activation heat capacity and nonlinearity in temperature dependence through correlated dynamical networks.

bioRxiv · Aug 21, 2020Biochemistry

Dynamical origins of heat capacity changes in enzyme catalysed reactions

M. W. van der Kamp, E. J. Prentice, K. L. Kraakman, M. Connolly, A. J. Mulholland, V. L. Arcus

The paper uses experiments and simulations to show that heat capacity changes in enzyme-catalyzed reactions can be predicted by molecular dynamics simulations, revealing dynamic changes beyond the active site.

bioRxiv · Jul 26, 2017Biochemistry