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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 3 Research Focus:chromatin & epigenetic regulation· 2 Organism:plant (other)· 2 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 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 E. Johansson· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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2 shared papersBiochemistry

A. Pabis

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3 papers

Recent·Most cited

BiochemistrybioRxivPreprintJul 1, 2023

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

V. Parkash, Y. Kulkarni, G. Bylund…·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.

DOI 10.1101/2023.07.01.547322

structural biologyexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivOct 30, 2018

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

J. R. Burke, J. J. LaClair, R. N. Philippe…·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.

DOI 10.1021/acscatal.9b01926

plant (other)structural biology

𝕏 PostBluesky

BiochemistrybioRxivAug 10, 2017

Evolution of chalcone isomerase from a non-catalytic ancestor

M. Kaltenbach, J. R. Burke, M. Dindo…·D. S. Tawfik

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

DOI 10.1038/s41589-018-0042-3

plant (other)structural biology

𝕏 PostBluesky