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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

Folding Lennard-Jones proteins by a contact potential.
C Clementi, M Vendruscolo, A Maritan, E Domany
– Proteins: Structure, Function, and Genetics
(2000)
37,
544
(doi: 10.1002/(SICI)1097-0134(19991201)37:4<544::AID-PROT5>3.0.CO;2-7)
Protein folding using contact maps
M Vendruscolo, E Domany
(2000)
171
(doi: 10.1016/s0083-6729(00)58025-x)
Comparison of two optimization methods to derive energy parameters for protein folding: Perceptron and Z score
M Vendruscolo, LA Mirny, EI Shakhnovich, E Domany
– Proteins Structure Function and Genetics
(2000)
41,
192
(doi: 10.1002/1097-0134(20001101)41:2<192::aid-prot40>3.0.co;2-3)
Neutral evolution of model proteins: Diffusion in sequence space and overdispersion
U Bastolla, HE Roman, M Vendruscolo
– Journal of Theoretical Biology
(1999)
200,
49
(doi: 10.1006/jtbi.1999.0975)
Hydrophobicity and unique folding of selected polymers
M Vendruscolo
– European Physical Journal B
(1999)
8,
323
(doi: 10.1007/s100510050695)
Protein Folding in Contact Map Space
M Vendruscolo, R Najmanovich, E Domany
– Physical Review Letters
(1999)
82,
656
(doi: 10.1103/PhysRevLett.82.656)
Protein folding using contact maps.
M Vendruscolo, E Domany
– VITAMINS AND HORMONES - ADVANCES IN RESEARCH AND APPLICATIONS, VOL 58
(1999)
58,
656
(doi: 10.1016/S0083-6729(00)58025-X)
Statistical properties of contact maps
M Vendruscolo, B Subramanian, I Kanter, E Domany, J Lebowitz
– Physical Review E
(1999)
59,
977
(doi: 10.1103/PhysRevE.59.977)
An optimal derivation of a potential for protein folding
M Vendruscolo
– Physica A: Statistical Mechanics and its Applications
(1999)
262,
35
(doi: 10.1016/s0378-4371(98)00358-6)
Pairwise contact potentials are unsuitable for protein folding
M Vendruscolo, E Domany
– The Journal of Chemical Physics
(1998)
109,
11101
(doi: 10.1063/1.477748)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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