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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

Transition states for protein folding have native topologies despite high structural variability.
K Lindorff-Larsen, M Vendruscolo, E Paci, CM Dobson
– Nature Structural & Molecular Biology
(2004)
11,
443
(doi: 10.1038/nsmb765)
Inhibition of protein crystallization by evolutionary negative design
JPK Doye, AA Louis, M Vendruscolo
– Physical Biology
(2004)
1,
(doi: 10.1088/1478-3967/1/1/P02)
Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein
K Lindorff-Larsen, S Kristjansdottir, K Teilum, W Fieber, CM Dobson, FM Poulsen, M Vendruscolo
– J Am Chem Soc
(2004)
126,
3291
(doi: 10.1021/ja039250g)
Inhibition of protein crystallization by evolutionary negative design.
JPK Doye, AA Louis, M Vendruscolo
– Physical biology.
(2004)
1,
P9
(doi: 10.1088/1478-3967/1/1/P02)
Statistical properties of neutral evolution.
U Bastolla, M Porto, HE Roman, M Vendruscolo
– Journal of molecular evolution
(2003)
57,
s103
(doi: 10.1007/s00239-003-0013-4)
Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints.
E Paci, CT Friel, K Lindorff-Larsen, SE Radford, M Karplus, M Vendruscolo
– Proteins: Structure, Function and Genetics
(2003)
54,
513
(doi: 10.1002/prot.10595)
Rare Fluctuations of Native Proteins Sampled by Equilibrium Hydrogen Exchange
M Vendruscolo, E Paci, CM Dobson, M Karplus
– J Am Chem Soc
(2003)
125,
15686
(doi: 10.1021/ja036523z)
Structures and relative free energies of partially folded states of proteins
M Vendruscolo, E Paci, M Karplus, CM Dobson
– Proceedings of the National Academy of Sciences
(2003)
100,
14817
(doi: 10.1073/pnas.2036516100)
Calculation of mutational free energy changes in transition states for protein folding.
K Lindorff-Larsen, E Paci, L Serrano, CM Dobson, M Vendruscolo
– Biophys J
(2003)
85,
1207
(doi: 10.1016/S0006-3495(03)74556-1)
Analysis of the distributed computing approach applied to the folding of a small beta peptide
E Paci, A Cavalli, M Vendruscolo, A Caflisch
– Proc Natl Acad Sci U S A
(2003)
100,
8217
(doi: 10.1073/pnas.1331838100)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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