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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

Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein.
S Gianni, C Camilloni, R Giri, A Toto, D Bonetti, A Morrone, P Sormanni, M Brunori, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2014)
111,
14141
(doi: 10.1073/pnas.1405233111)
Identification and characterization of PKCγ, a kinase associated with SCA14, as an amyloidogenic protein
H Takahashi, N Adachi, T Shirafuji, S Danno, T Ueyama, M Vendruscolo, AN Shuvaev, T Sugimoto, T Seki, D Hamada, K Irie, H Hirai, N Sakai, N Saito
– Human Molecular Genetics
(2014)
24,
525
(doi: 10.1093/hmg/ddu472)
Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts
W Boomsma, P Tian, J Frellsen, J Ferkinghoff-Borg, T Hamelryck, K Lindorff-Larsen, M Vendruscolo
– Proc Natl Acad Sci U S A
(2014)
111,
13852
(doi: 10.1073/pnas.1404948111)
NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain
HTA Leung, P Kukic, C Camilloni, F Bemporad, A De Simone, FA Aprile, JR Kumita, M Vendruscolo
– Protein Sci
(2014)
23,
1596
(doi: 10.1002/pro.2538)
Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain.
F Blombach, H Launay, APL Snijders, V Zorraquino, H Wu, B de Koning, SJJ Brouns, TJG Ettema, C Camilloni, A Cavalli, M Vendruscolo, MJ Dickman, LD Cabrita, A La Teana, D Benelli, P Londei, J Christodoulou, J van der Oost
– The Biochemical journal
(2014)
462,
373
(doi: 10.1042/BJ20131474)
Cyclophilin a catalyzes proline isomerization by an electrostatic handle mechanism
C Camilloni, AB Sahakyan, MJ Holliday, NG Isern, F Zhang, EZ Eisenmesser, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2014)
111,
10203
(doi: 10.1073/pnas.1404220111)
Statistical mechanics of the denatured state of a protein using replica-averaged metadynamics.
C Camilloni, M Vendruscolo
– Journal of the American Chemical Society
(2014)
136,
8982
(doi: 10.1021/ja5027584)
A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings
C Camilloni, M Vendruscolo
– The Journal of Physical Chemistry B
(2014)
119,
653
(doi: 10.1021/jp5021824)
ALMOST: An all atom molecular simulation toolkit for protein structure determination
B Fu, AB Sahakyan, C Camilloni, GG Tartaglia, E Paci, A Caflisch, M Vendruscolo, A Cavalli
– Journal of Computational Chemistry
(2014)
35,
1101
(doi: 10.1002/jcc.23588)
Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour.
G Fusco, A De Simone, T Gopinath, V Vostrikov, M Vendruscolo, CM Dobson, G Veglia
– Nature Communications
(2014)
5,
3827
(doi: 10.1038/ncomms4827)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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