Author

G. Courtade

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:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Organism:fungi (other)· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:structural biology· 1

Frequent Co-Authors

F. L. Aachmann· 3 shared V. G. H. Eijsink· 3 shared A. Stepnov· 2 shared K. Lindorff-Larsen· 2 shared Y. Wang· 2 shared Z. Forsberg· 2 shared A. Niebisch· 1 shared E. Buchinger· 1 shared

Activity by Year

2021-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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3 shared papersBiochemistry

F. L. Aachmann

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Author profile →

4 papers

Recent·Most cited

The effect of linker conformation on performance and stability of a two-domain lytic polysaccharide monooxygenase

Z. Forsberg, A. Stepnov, G. Tesei, Y. Wang, E. Buchinger, S. K. Kristiansen, F. L. Aachmann, L. Arleth, V. G. H. Eijsink, K. Lindorff-Larsen, G. Courtade

This study investigates how linker conformation affects the performance and stability of a two-domain lytic polysaccharide monooxygenase by analyzing wild-type and engineered variants.

bioRxiv · Jun 1, 2023Biochemistry

Biochemical characterization and NMR study of a PET-hydrolyzing cutinase from Fusarium solani pisi

K. N. Hellesnes, S. Vijayaraj, P. Fojan, E. Petersen, G. Courtade

This study characterizes a PET-hydrolyzing cutinase from Fusarium solani pisi, identifying key interactions and factors affecting its catalytic performance on PET.

Biochemistry · Mar 27, 2023Peer-reviewedBiochemistry

Following the fate of lytic polysaccharide monooxygenases (LPMOs) under oxidative conditions by NMR spectroscopy

I. A. Christensen, V. G. H. Eijsink, A. Stepnov, G. Courtade, F. L. Aachmann

This study uses NMR spectroscopy to investigate how oxidative conditions affect the structure and activity of the chitin-active LPMO SmLPMO10A, showing substrate protection against oxidative damage.

bioRxiv · Feb 2, 2023 · PreprintBiochemistry

NMR structures and functional roles of two related chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus

E. Madland, Z. Forsberg, Y. Wang, K. Lindorff-Larsen, A. Niebisch, J. Modregger, V. G. H. Eijsink, F. L. Aachmann, G. Courtade

This study determines the NMR structures of two chitin-binding domains from CjLPMO10A and shows functional differences in their chitin-binding affinities and substrate specificity.

bioRxiv · Apr 25, 2021Biochemistry