Author

S. C. L. Kamerlin

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:chromatin & epigenetic regulation· 3 Assay:structural biology· 3 Organism:plant (other)· 2 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Assay:protein sequence· 1 Assay:protein structure· 1

Frequent Co-Authors

A. Pabis· 2 shared D. S. Tawfik· 2 shared J. P. Noel· 2 shared J. R. Burke· 2 shared M. Kaltenbach· 2 shared A. Rabin· 1 shared A. T. Nelson· 1 shared C. Jackson· 1 shared

Activity by Year

2017-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersBiochemistry

A. Pabis

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Author profile →

4 papers

Recent·Most cited

A sensor complements the steric gate when DNA polymerase ϵ discriminates ribonucleotides.

V. Parkash, Y. Kulkarni, G. Bylund, P. Osterman, S. C. L. Kamerlin, E. Johansson

This study identifies a sensor in the finger domain of DNA polymerase ϵ that complements the steric gate in discriminating ribonucleotides from deoxyribonucleotides.

bioRxiv · Jul 1, 2023 · PreprintBiochemistry

Higher-order epistatic networks underlie the evolutionary fitness landscape of a xenobiotic- degrading enzyme

G. Yang, D. W. Anderson, F. Baier, E. Dohmen, N. Hong, P. D. Carr, S. C. L. Kamerlin, C. Jackson, E. Bornberg-Bauer, N. Tokuriki

This study identifies five mutations that enable the evolution of a xenobiotic-degrading enzyme and shows that higher-order epistasis shapes its adaptive landscape and substrate specificity.

bioRxiv · Dec 26, 2018 · PreprintBiochemistry

Bifunctional Substrate Activation via an Arginine Residue Drives Catalysis in Chalcone Isomerases

J. R. Burke, J. J. LaClair, R. N. Philippe, A. Pabis, J. M. Jez, G. A. Cortina, M. Kaltenbach, M. E. Bowman, G. V. Louie, K. B. Woods, A. T. Nelson, D. S. Tawfik, S. C. L. Kamerlin, J. P. Noel

The paper elucidates the catalytic mechanism of chalcone isomerases, showing how an arginine residue activates substrates via Bronsted and Lewis acid interactions, and highlights structural differences between type-1 and type-2 enzymes.

bioRxiv · Oct 30, 2018Biochemistry

Evolution of chalcone isomerase from a non-catalytic ancestor

M. Kaltenbach, J. R. Burke, M. Dindo, A. Pabis, F. S. Munsberg, A. Rabin, S. C. L. Kamerlin, J. P. Noel, D. S. Tawfik

This study shows chalcone isomerase evolved from a non-catalytic ancestor through four founder mutations with weak epistasis, enabling enantioselective activity.

bioRxiv · Aug 10, 2017Biochemistry