skip to content
Home

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

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
– Nat Commun
(2014)
5,
3827
(doi: 10.1038/ncomms4827)
The amyloid state and its association with protein misfolding diseases.
TPJ Knowles, M Vendruscolo, CM Dobson
– Nature reviews. Molecular cell biology
(2014)
15,
384
(doi: 10.1038/nrm3810)
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation
AK Buell, C Galvagnion, R Gaspar, E Sparr, M Vendruscolo, TPJ Knowles, S Linse, CM Dobson
– Proceedings of the National Academy of Sciences of the United States of America
(2014)
111,
7671
(doi: 10.1073/pnas.1315346111)
Understanding the influence of codon translation rates on cotranslational protein folding
EP O'Brien, P Ciryam, M Vendruscolo, CM Dobson
– Accounts of Chemical Research
(2014)
47,
1536
(doi: 10.1021/ar5000117)
Determination of the Individual Roles of the Linker Residues in the Inter-Domain Motions of Calmodulin using NMR Chemical Shifts
P Kukic, C Camilloni, A Cavalli, M Vendruscolo
– Journal of Molecular Biology
(2014)
106,
636A
(doi: 10.1016/j.jmb.2014.02.002)
New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics
R Montalvao, C Camilloni, A De Simone, M Vendruscolo
– Journal of Biomolecular NMR
(2014)
58,
233
(doi: 10.1007/s10858-013-9801-3)
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)
Spatial propagation of protein polymerization
SIA Cohen, L Rajah, CH Yoon, AK Buell, DA White, RA Sperling, M Vendruscolo, EM Terentjev, CM Dobson, DA Weitz, TPJ Knowles
– Phys Rev Lett
(2014)
112,
098101
(doi: 10.1103/PhysRevLett.112.098101)
  • <
  • 48 of 80
  • >

Research Groups

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk

    Study at Cambridge

    About the University

    Research at Cambridge