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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

Analysis of the Contributions of Ring Current and Electric Field Effects to the Chemical Shifts of RNA Bases
AB Sahakyan, M Vendruscolo
– The journal of physical chemistry. B
(2013)
117,
1989
(doi: 10.1021/jp3057306)
Assessment of the use of NMR chemical shifts as replica-averaged structural restraints in molecular dynamics simulations to characterize the dynamics of proteins.
C Camilloni, A Cavalli, M Vendruscolo
– The journal of physical chemistry. B
(2013)
117,
1838
(doi: 10.1021/jp3106666)
Sequence-Based Prediction of Protein Behavior
GG Tartaglia, M Vendruscolo
(2013)
167
(doi: 10.1002/9783527654185.ch9)
The Kinetics and Mechanisms of Amyloid Formation
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
(2013)
183
(doi: 10.1002/9783527654185.ch10)
Structure of a Misfolded Intermediate of a PDZ Domain
A De Simone, S Gianni, M Vendruscolo
– Bio-nanoimaging: Protein Misfolding and Aggregation
(2013)
463
(doi: 10.1016/B978-0-12-394431-3.00041-9)
Characterization of Free Energy Landscapes of Proteins using NMR Spectroscopy
M Vendruscolo
– Biophysical Journal
(2013)
104,
45A
(doi: 10.1016/j.bpj.2012.11.287)
MD simulations of intrinsically disordered proteins with replica-averaged chemical shift restraints
B Fu, C Camilloni, A Cavalli, M Vendruscolo
– EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2013)
42,
S188
(link to publication)
In Vivo Translation Rates Can Substantially Delay the Co-Translational Folding of the E. Coli Cytosolic Proteome
P Ciryam, RI Morimoto, M Vendruscolo, CM Dobson, EP O'Brien
– Biophysical Journal
(2013)
104,
578a
(doi: 10.1016/j.bpj.2012.11.3207)
Thermodynamics of an Intrinsically Disordered Protein by Atomistic Simulations
D Granata, FB Baghal, C Camilloni, M Vendruscolo, A Laio
– Biophysical Journal
(2013)
104,
55a
(doi: 10.1016/j.bpj.2012.11.344)
In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome.
P Ciryam, RI Morimoto, M Vendruscolo, CM Dobson, EP O'Brien
– Proc Natl Acad Sci U S A
(2012)
110,
E132
(doi: 10.1073/pnas.1213624110)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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