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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

Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions.
EP O'Brien, J Christodoulou, M Vendruscolo, CM Dobson
– Journal of the American Chemical Society
(2012)
134,
10920
(doi: 10.1021/ja302305u)
Prediction of variable translation rate effects on cotranslational protein folding.
EP O'Brien, M Vendruscolo, CM Dobson
– Nature Communications
(2012)
3,
868
(doi: 10.1038/ncomms1850)
Fibrillogenic propensity of the GroEL apical domain: A Janus-faced minichaperone
J Chen, H Yagi, P Sormanni, M Vendruscolo, K Makabe, T Nakamura, Y Goto, K Kuwajima
– FEBS Letters
(2012)
586,
1120
(doi: 10.1016/j.febslet.2012.03.019)
Structure of an intermediate state in protein folding and aggregation.
P Neudecker, P Robustelli, A Cavalli, P Walsh, P Lundström, A Zarrine-Afsar, S Sharpe, M Vendruscolo, LE Kay
– Science (New York, N.Y.)
(2012)
336,
362
(doi: 10.1126/science.1214203)
1H, 13C and 15N resonance assignments of human muscle acylphosphatase
G Fusco, A De Simone, STD Hsu, F Bemporad, M Vendruscolo, F Chiti, CM Dobson
– Biomolecular NMR Assignments
(2012)
6,
27
(doi: 10.1007/s12104-011-9318-1)
Proteome folding and aggregation
M Vendruscolo
– Current Opinion in Structural Biology
(2012)
22,
138
(doi: 10.1016/j.sbi.2012.01.005)
Fibrillogenic propensity of the GroEL apical domain: A Janus-faced minichaperone
J Chen, H Yagi, P Sormanni, M Vendruscolo, K Makabe, T Nakamura, Y Goto, K Kuwajima
– FEBS Lett
(2012)
586,
1120
(doi: 10.1016/j.febslet.2012.03.019)
From macroscopic measurements to microscopic mechanisms of protein aggregation.
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
– Journal of Molecular Biology
(2012)
421,
160
(doi: 10.1016/j.jmb.2012.02.031)
Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts.
C Camilloni, A De Simone, WF Vranken, M Vendruscolo
– Biochemistry
(2012)
51,
2224
(doi: 10.1021/bi3001825)
Characterization of the Conformational Equilibrium between the Two Major Substates of RNase A Using NMR Chemical Shifts
C Camilloni, P Robustelli, A De Simone, A Cavalli, M Vendruscolo
– Journal of the American Chemical Society
(2012)
134,
3968
(doi: 10.1021/ja210951z)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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