Author

K. L. Kraakman

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· 2

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Approach:experimental assay· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

A. J. Mulholland· 2 shared E. J. Prentice· 2 shared M. W. van der Kamp· 2 shared V. L. Arcus· 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 · 45 mutual co-author links

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2 shared papersBiochemistry

A. J. Mulholland

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2 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

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