Robbert Kim

Research:

I am a structural biologist and have spent most of my professional life on the structural elucidation of enzymes and investigating their enzymatic activity. Combining structural and activity studies of enzymes can generate mechanistic insight into the biological activity mechanism, but can also indicate possibilities for human intervention. Currently I am establishing the <LINK>Protein Centre</LINK> which helps researchers to express their protein of interest as well as analyzing them using various biophysical methods. At the Chemical Immunology group I mostly study DUBs; combining the in-house developed chemical tools with the expression and purification facility to get insight into activity mechanisms and inhibition possibilities.

Curriculum Vitae:

I obtained my Bachelor’s degree in Chemistry in 2010 and my Master’s degree in Molecular and Cellular Life Sciences in 2012 at Utrecht University. After my Master’s I continued to work as a research associate with Gideon Davies at the York Structural Biology Laboratory, working on the structural elucidation of enzymes. During my PhD at the Netherlands Cancer Institute at the group of Titia Sixma I followed this research theme, working on deubiquitinating enzymes. In my PhD I used different biophysical techniques, supplemented with structural biology and biochemistry, to elucidate the activity mechanism of USP7. In 2018 I joined the Ovaa group to set up a protein facility, focusing on the production and analysis of proteins for members of our institute.

Publications

  • Structure of USP7 catalytic domain and three Ubl-domains reveals a connector α-helix with regulatory role.

    Kim, R.Q., van Dijk, W.J. and Sixma, T.K.;

    Journal of Structural Biology 195 2016, 11–8. https://doi.org/10.1016/j.jsb.2016.05.005

  • Structural enzymology of Helicobacter pylori methylthioadenosine nucleosidase in the futalosine pathway.

    Kim, R.Q., Offen, W.A., Davies, G.J. and Stubbs, K.A.;

    Acta Crystallographica Section D, Biological Crystallography 70 2014, 177–85. https://doi.org/10.1107/S1399004713026655.

  • The copper active site of CBM33 polysaccharide oxygenases.

    Hemsworth, G.R., Taylor, E.J., Kim, R.Q., Gregory, R.C., Lewis, S.J., Turkenburg, J.P., Parkin, A., Davies, G.J. and Walton, P.H.;

    Journal of the American Chemical Society 135 2013, 6069–77. https://doi.org/10.1021/ja402106e.

Groups

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