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Centre for Misfolding Diseases

Karen Stroobants is a post-doctoral researcher in the Centre for Protein Misfolding Diseases at the Chemistry Department of the University of Cambridge. With a strong background in biophysical characterisation of proteins, she recently engaged in the study of membrane protein aggregates and their potential role in neurodegenerative diseases. The formation of aggregates has been identified as a crucial common feature in disorders such as Alzheimer’s and Parkinson’s diseases, and amyloid formation was studied extensively for few specific associated proteins. More recently, widespread aggregation of numerous other proteins, with high vulnerabilities for aggregation, was proposed to contribute to the disease progression. Membrane proteins are among the most aggregation prone proteins and those in the respiratory chain and glucose metabolism were previously associated to pathological pathways. Karen's current research envisions the biophysical characterisation of membrane protein aggregates as well as the establishment of their potential role in neurodegenerative disease pathways.

Publications

Amyloid-like Fibrils from an α‑Helical Transmembrane Protein
K Stroobants, JR Kumita, NJ Harris, DY Chirgadze, CM Dobson, PJ Booth, M Vendruscolo
– Biochemistry
(2017)
56,
3225
MARIO MOLINA
M Molina, J Fenton, K Stroobants, T Gianetti
– NATURE
(2017)
550,
S63
Probing Polyoxometalate–Protein Interactions Using Molecular Dynamics Simulations
A Solé-Daura, V Goovaerts, K Stroobants, G Absillis, P Jiménez-Lozano, JM Poblet, JD Hirst, TN Parac-Vogt, JJ Carbó
– Chemistry – A European Journal
(2016)
22,
15157
Probing Polyoxometalate-Protein Interactions Using Molecular Dynamics Simulations.
A Solé-Daura, V Goovaerts, K Stroobants, G Absillis, P Jiménez-Lozano, JM Poblet, JD Hirst, TN Parac-Vogt, JJ Carbó
– Chemistry – A European Journal
(2016)
22,
15280
Eu(III) luminescence and tryptophan fluorescence spectroscopy as a tool for understanding interactions between hen egg white lysozyme and metal-substituted Keggin type polyoxometalates
V Goovaerts, K Stroobants, G Absillis, TN Parac-Vogt
– Journal of inorganic biochemistry
(2015)
150,
72
Polyoxometalate reactivity toward biomolecules and their model systems
K Stroobants, G Absillis, TN Parac-Vogt
(2015)
171
Thermodynamic study of the interaction between hen egg white lysozyme and Ce(iv)-Keggin polyoxotungstate as artificial protease
K Stroobants, D Saadallah, G Bruylants, TN Parac-Vogt
– Physical chemistry chemical physics : PCCP
(2014)
16,
21778
Molecular origin of the hydrolytic activity and fixed regioselectivity of a Zr(IV) -substituted polyoxotungstate as artificial protease
K Stroobants, V Goovaerts, G Absillis, G Bruylants, E Moelants, P Proost, TN Parac-Vogt
– Chemistry (Weinheim an der Bergstrasse, Germany)
(2014)
20,
9567
Molecular origin of the hydrolytic activity and fixed regioselectivity of a ZrIV-substituted polyoxotungstate as artificial protease
K Stroobants, V Goovaerts, G Absillis, G Bruylants, E Moelants, P Proost, TN Parac-Vogt
– Chemistry (Weinheim an der Bergstrasse, Germany)
(2014)
20,
9567
Selective hydrolysis of hen egg white lysozyme at Asp-X peptide bonds promoted by oxomolybdate.
K Stroobants, PH Ho, E Moelants, P Proost, TN Parac-Vogt
– Journal of Inorganic Biochemistry
(2014)
136,
73
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Telephone number

01223 761083