Author

E. J. Koers

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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Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 3 Approach:biophysical modeling· 1 Research Focus:drug response / drug discovery· 1 Assay:proteomics· 1

Frequent Co-Authors

D. A. Sykes· 2 shared S. J. Tans· 2 shared A. Kaur· 1 shared A. Mashaghi· 1 shared A. Roth· 1 shared B. L. Hoare· 1 shared C. R. Harwood· 1 shared D. B. Veprintsev· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiophysics

D. A. Sykes

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Author profile →

4 papers

Recent·Most cited

Probing drug-target engagement of soluble Gαi1 protein using the SolThermoBRET thermal shift assay

O. Brod, D. Plevako, T. Perera, P. Hompluem, E. J. Koers, M. Hilbert, D. A. Sykes, D. Veprintsev

This paper introduces a high-throughput BRET-based thermal shift assay to measure protein stability and ligand interactions with Gi1 protein without purification.

bioRxiv · Feb 15, 2024 · PreprintBiophysics

Direct observation of Hsp90-induced compaction in a protein chain

A. Mashaghi, F. Moayed, E. J. Koers, G. Kramer, M. P. Mayer, S. J. Tans

This study uses optical tweezers to show Hsp90 induces local contractions in unfolded protein chains, leading to global compaction and suppression of misfolding and aggregation.

bioRxiv · Aug 8, 2021Biophysics

ThermoBRET: a ligand-engagement nanoscale thermostability assay applied to GPCRs

B. L. Hoare, D. N. Tippett, A. Kaur, S. A. Cullum, T. Miljus, E. J. Koers, C. R. Harwood, N. Dijon, N. D. Holliday, D. A. Sykes, D. B. Veprintsev

ThermoBRET quantifies GPCR thermostability using BRET without labelled ligands, revealing ligand effects on protein unfolding in non-purified samples.

bioRxiv · Aug 5, 2020Biochemistry

Polypeptide collapse modulation and folding stimulation by GroEL-ES

M. M. Naqvi, M. J. Avellaneda, A. Roth, E. J. Koers, V. Sunderlikova, G. J. Kramer, H. S. Rye, S. J. Tans

This study shows GroEL-ES enhances polypeptide collapse, directly stimulating folding by pulling chains into its cavity and promoting compaction and folding transitions.

bioRxiv · Jun 17, 2020 · PreprintBiophysics