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Karen Stroobants

Researcher at University of Cambridge

Publications -  18
Citations -  563

Karen Stroobants is an academic researcher from University of Cambridge. The author has contributed to research in topics: Quenching (fluorescence) & Nuclear magnetic resonance spectroscopy. The author has an hindex of 11, co-authored 17 publications receiving 467 citations. Previous affiliations of Karen Stroobants include Katholieke Universiteit Leuven.

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Polyoxometalates as a novel class of artificial proteases: selective hydrolysis of lysozyme under physiological pH and temperature promoted by a cerium(IV) Keggin-type polyoxometalate.

TL;DR: NMR spectroscopy titration experiments showed that on protein addition the intensity of the (31)P NMR signal of 1 gradually decreased due to the formation of a large protein/polyoxometalate complex and completely disappeared when the HEWL/1 ratio reached 1:2.
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Regioselective Hydrolysis of Human Serum Albumin by ZrIV-Substituted Polyoxotungstates at the Interface of Positively Charged Protein Surface Patches and Negatively Charged Amino Acid Residues

TL;DR: Findings suggest an electrostatic nature of the observed reactivity ofcomplexes comprising the Lewis acidic Zr(IV) metal and protein binding polyoxotungstate ligands of Lindqvist-, Keggin- and Wells-Dawson-type.
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Molecular interactions between serum albumin proteins and Keggin type polyoxometalates studied using luminescence spectroscopy

TL;DR: The interaction between the plenary KeggIn H3PW12O40, lacunary Keggin K7PW11O39 and the Eu(III) type polyoxometalates (POMs), and the proteins human and bovine serum albumin (HSA and BSA) was studied using steady state and time-resolved Eu (III) luminescence and tryptophan (Trp) fluorescence spectroscopy.
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Molecular Origin of the Hydrolytic Activity and Fixed Regioselectivity of a ZrIV-Substituted Polyoxotungstate as Artificial Protease

TL;DR: A multitechnique approach has been applied in order to identify the thermodynamic and kinetic parameters related to the regioselective hydrolysis of human serum albumin promoted by the Wells-Dawson polyoxometalate (POM), K15 H[Zr(α2 -P2 W17 O61 )2 ].
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Probing Polyoxometalate-Protein Interactions Using Molecular Dynamics Simulations.

TL;DR: The CeK anion shows higher protein affinity than the CeK2 and ZrL anions, because it is less hydrophilic and it has the right size and shape for establishing interactions with several residues simultaneously.