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Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

Professor of Biophysics

Our research

In the last 15 years our research has been focused on the development of methods of characterising the structure, dynamics and interactions of proteins in previously inaccessible states. These methods are based on the use of experimental data, in particular from nuclear magnetic resonance spectroscopy, as structural restraints in molecular dynamics simulations. Through this approach it is possible to obtain information about a variety of protein conformations, as for example those populated during the folding process, and about protein interactions in complex environments, including those generating aggregate species that are associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases.

Application to neurodegenerative diseases

More recently, these studies have led us to investigate the physico-chemical principles of proteins homeostasis and their application to the development of therapeutic strategies against neurodegenerative diseases. Starting from the observation that proteins are expressed in the cell at levels close to their solubility limits, we are developing approaches to prevent or delay misfolding disorders based on the enhancement of our quality control mechanisms against protein aggregation.

Watch Professor Vendruscolo discuss his research

Take a tour of the Una Finlay Laboratory in the Centre for Misfolding Diseases

Publications

Chromatin Unfolding by Epigenetic Modifications Explained by Dramatic Impairment of Internucleosome Interactions: A Multiscale Computational Study.
R Collepardo-Guevara, G Portella, M Vendruscolo, D Frenkel, T Schlick, M Orozco
– J Am Chem Soc
(2015)
137,
10205
(doi: 10.1021/jacs.5b04086)
A Rational Design Strategy for the Selective Activity Enhancement of a Molecular Chaperone toward a Target Substrate.
FA Aprile, P Sormanni, M Vendruscolo
– Biochemistry
(2015)
54,
5103
(doi: 10.1021/acs.biochem.5b00459)
Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins
P Sormanni, FA Aprile, M Vendruscolo
– Proc Natl Acad Sci U S A
(2015)
112,
9902
(doi: 10.1073/pnas.1422401112)
Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy
Y Pustovalova, P Kukic, M Vendruscolo, DM Korzhnev
– Biochemistry
(2015)
54,
4611
(doi: 10.1021/acs.biochem.5b00345)
Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution
KD Brewer, T Bacaj, A Cavalli, C Camilloni, JD Swarbrick, J Liu, A Zhou, P Zhou, N Barlow, J Xu, AB Seven, EA Prinslow, R Voleti, D Häussinger, AMJJ Bonvin, DR Tomchick, M Vendruscolo, B Graham, TC Südhof, J Rizo
– Nature Structural and Molecular Biology
(2015)
22,
555
(doi: 10.1038/nsmb.3035)
Constructing free energy landscapes of RNAs at atomic resolution and characterisation of their excited states
AN Borkar, P Vallurupalli, C Camilloni, LE Kay, M Vendruscolo
– Journal of Biomolecular Structure and Dynamics
(2015)
33,
56
(doi: 10.1080/07391102.2015.1032706)
89 Constructing free energy landscapes of RNAs at atomic resolution and characterisation of their excited states.
AN Borkar, P Vallurupalli, C Camilloni, LE Kay, M Vendruscolo
– Journal of biomolecular structure & dynamics
(2015)
33,
58
(doi: 10.1080/07391102.2015.1032706)
Reply to "Comment on 'A Tensor-Free Method for the Structural and Dynamic Refinement of Proteins using Residual Dipolar Couplings'".
C Camilloni, M Vendruscolo
– J Phys Chem B
(2015)
119,
8225
(doi: 10.1021/acs.jpcb.5b04166)
Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution.
KD Brewer, T Bacaj, A Cavalli, C Camilloni, JD Swarbrick, J Liu, A Zhou, P Zhou, N Barlow, J Xu, AB Seven, EA Prinslow, R Voleti, D Häussinger, AMJJ Bonvin, DR Tomchick, M Vendruscolo, B Graham, TC Südhof, J Rizo
– Nature structural & molecular biology
(2015)
22,
555
(doi: 10.1038/nsmb.3035)
Analysis of the performance of the CHESHIRE and YAPP methods at CASD-NMR round 3
A Cavalli, M Vendruscolo
– Journal of Biomolecular NMR
(2015)
62,
503
(doi: 10.1007/s10858-015-9940-9)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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