Author

M. Ubbink

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· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:bacteria (other)· 2 Research Focus:protein folding & dynamics· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1

Frequent Co-Authors

F. Ben Bdira· 4 shared A. N. Volkov· 3 shared H. S. Overkleeft· 2 shared R. T. Dame· 2 shared A. Cramer-Blok· 1 shared A. L. Boyle· 1 shared A. M. Erkelens· 1 shared A. M. Lippa· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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4 shared papersBiochemistry

F. Ben Bdira

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Author profile →

5 papers

Recent·Most cited

Novel anti-repression mechanism of H-NS proteins by a phage "early protein".

F. Ben Bdira, L. Qing, A. N. Volkov, A. M. Lippa, A. M. Erkelens, N. Bowring, A. L. Boyle, M. Ubbink, S. L. Dove, R. T. Dame

This study identifies how phage gp4 modulates H-NS protein MvaT by stabilizing its half-open conformation, relieving gene silencing and affecting P. aeruginosa growth.

bioRxiv · Mar 3, 2021Biochemistry

Tuning the transglycosylation reaction of a GH11 xylanase by a delicate enhancement of its thumb flexibility

K. Marneth, H. van den Elst, A. Cramer-Blok, J. D. C. Codee, H. S. Overkleeft, H. M. F. G. Aerts, M. Ubbink, F. Ben Bdira

This study modifies a GH11 xylanase to enhance transglycosylation by increasing thumb flexibility through a point mutation, altering its enzymatic balance and dynamics.

bioRxiv · Dec 19, 2020Biochemistry

The MPS1 kinase NTE region has helical propensity and preferred conformations towards the TPR domain

Y. Hiruma, M.-T. Matsoukas, W. Touw, G. Spyroulias, G. Kops, M. Ubbink, A. Perrakis

This study investigates the conformational dynamics of the MPS1 kinase NTE region relative to the TPR domain using paramagnetic NMR and Rosetta, revealing helical propensity and convex surface interactions.

bioRxiv · Mar 31, 2020 · PreprintBiochemistry

Catalysis by a rigid enzyme

F. Ben Bdira, C. A. Waudby, A. N. Volkov, S. Schroder, E. AB, J. Codee, H. S. Overkleeft, H. Aerts, H. van Ingen, M. Ubbink

The paper shows that the rigid xylanase enzyme uses substrate flexibility to facilitate catalysis without significant structural changes.

bioRxiv · Oct 24, 2019 · PreprintBiochemistry

Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins

L. Qin, F. Ben Bdira, Y. G. J. Sterckx, A. N. Volkov, J. Vreede, G. Giachin, P. van Schaik, M. Ubbink, R. T. Dame

This study identifies the molecular mechanism by which H-NS proteins switch DNA binding states in response to osmotic changes, showing that ionic strength affects electrostatic interactions between domains.

bioRxiv · Sep 5, 2019Biochemistry