Research Programmes
Chemistry & Molecular Pharmacology
Laboratory of Molecular Biophysics
Xavier Salvatella
Group Leader
ICREA Researcher
Office Tel : +34 93 40 20459
Lab Tel : +34 93 402 04 61
e-mail : xavier.salvatella
irbbarcelona.org
Background
A high resolution description of the structure and dynamics of proteins is a very useful tool to study the properties and the function of these important biomacromolecules and, most importantly, to understand how changes in sequence or environment can lead to disease. The research work carried out at the Laboratory of Molecular Biophysics aims, on the one hand, at developing methods to probe the fluctuations of the structure of proteins by combining experimental data and molecular simulations and, on the other hand, at understanding how changes in such motions relate to the molecular recognition of proteins, to their function and disease.
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Laboratory of Molecular Biophysics
Population of non-native states of lysozyme variants drives amyloid fibril formation.
Büll A, Dhulesia A, Mossuto M, Cremades N, Kumita J, Dumoulin M, Welland M, Knowles T, Salvatella X, Dobson C M
J Am Chem Soc, 133 (20), 7737-7743 (2011)
Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition
Fenwick R. B., Esteban-Martín S, Richter B, Lee D, Walter K. F. A, Milovanovic D, Becker S, Lakomek N. A, Griesinger C and Salvatella X
J Am Chem Soc, 133 (27), 10336-10339 (2011)
Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein
Mossuto M F, Bolognesi B, Guixer B, Dhulesia A, Agostini F, Janet R, Kumita J R, Tartaglia G G, Dumoulin M, Dobson C M and Salvatella X
Angew Chem Intl Ed, 50 (31), 7048-7051 (2011)
Refinement of ensembles describing unstructured proteins using NMR residual dipolar couplings.
Esteban-Martín S, Fenwick RB and Salvatella X.
J Am Chem Soc., 132 (13), 4626-4632 (2010)
Time averaging of NMR chemical shifts in the MLF peptide in the solid state
De Gortari I, Portella G, Salvatella X, Bajaj VS, van der Wel PCA, Yates JR, Segall MD, Pickard CJ, Payne MC and Vendruscolo M.
J Am Chem Soc, 132, 5993-6000 (2010)
The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity
Mossuto MF, Dhulesia A, Devlin G, Frare E, Kumita JR, Polverino de Laureto P, Dumoulin M, Fontana A, Dobson CM and Salvatella X.
J Mol Biol, 402, 783-796 (2010)
Local cooperativity in the amyloidogenic state of human lysozyme observed at atomic resolution
Dhulesia A, Cremades N, Kumita J, Hsu ST, Mossuto M, Dumoulin M, Nietlispach D, Akke M, Salvatella X and Dobson CM.
J Am Chem Soc 132, 15580-15588 (2010)
Influence of experimental uncertainties on the properties of ensembles derived from NMR residual dipolar couplings
Fenwick RB, Esteban-Martín S and Salvatella X.
J Phys Chem Lett 1, 3438-3441 (2010)
Towards an accurate description of free energies in solution states of proteins
De Simone A, Richter B, Salvatella X and Vendruscolo M
J Am Chem Soc, 131, 3810-3811 (2009)
Position-dependent electrostatic protection against protein aggregation
Buell A, Tartaglia GG, Birkett NR, Waudby CA, Vendruscolo M, Salvatella X, Welland ME, Dobson CM and Knowles T
ChemBioChem, 10 (8), 1309-1312 (2009)
Folding of small proteins by monte carlo simulations with chemical shift restraints without the use of molecular fragment replacement or structural homology
Robustelli P, Cavalli A, Dobson CM, Vendruscolo M and Salvatella X
J Phys Chem B 113, 7890-7896 (2009)
Fast and accurate predictions of protein NMR chemical shifts from interatomic distances
Kohlhoff KJ, Robustelli P, Cavalli A, Salvatella X and Vendruscolo M
J Am Chem Soc, 131 (39), 13894-13895 (2009)
Influence of the fluctuations of the alignment tensor on the analysis of the structure and dynamics of proteins using residual dipolar couplings
Salvatella X, Richter B and Vendruscolo M
J Biomol NMR, 40 (1), 71-81 (2008)
Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation
Calloni G, Lendel S, Campioni S, Gianinni S, Gliozzi A, Relini A, Vendruscolo M, Dobson CM, Salvatella X and Chiti F
J Am Chem Soc, 130 (39), 13040-13050 (2008)
Structure determination of protein-protein complexes using NMR chemical shifts: Case of an endonuclease colicin-immunity protein complex
Montalvao RW, Cavalli A, Salvatella X, Blundell TL and Vendruscolo M
J Am Chem Soc, 130, 15990-15996 (2008)
Conformational properties of the aggregation precursor state of HypF-N
Campioni S, Mossuto MF, Torrassa S, Calloni G, de Laureto PP, Relini A, Fontana A and Chiti F
J Mol Biol, 379 (3), 554-567 (2008)
Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values
Geierhaas CD, Salvatella X, Clarke J and Vendruscolo M
Protein Eng Des Sel, 21 (3), 215-222 (2008)
Structural analysis of substance P using molecular dynamics and NMR spectroscopy
Corcho FJ, Salvatella X, Canto J, Giralt E and Perez JJ
J Pept Sci, 13 (11), 728-741 (2007)
Protein structure determination from NMR chemical shifts
Cavalli A, Salvatella X, Dobson CM and Vendruscolo M
Proc Natl Acad Sci USA, 104 (23), 9615-9620 (2007)
The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins
Richter B, Gsponer J, Várnai P, Salvatella X and Vendruscolo M
J Biomol NMR, 37 (2), 117-135 (2007)
Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values
Salvatella X, Dobson CM, Fersht AR and Vendruscolo M
Proc Natl Acad Sci USA, 102 (35), 12389-12394 (2005)
A new class of foldamers based on cis-gamma-amino-L-proline
Farrera-Sinfreu J, Zaccaro L, Vidal D, Salvatella X, Giralt E, Pons M, Albericio F and Royo M
J Am Chem Soc, 126 (19), 6048-6057 (2004)
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM and Kay LE
Nature, 430 (6999), 586-590 (2004)
A tetraguanidinium ligand binds to the surface of the tetramerization domain of protein P53
Salvatella X, Martinell M, Gairí M, Mateu MG, Feliz M, Hamilton AD, De Mendoza J and Giralt E
Angew Chem Int Ed Engl, 43 (2), 196-198 (2004)
NMR-based methods and strategies for drug discovery
Salvatella X and Giralt E
Chem Soc Rev, 32 (6), 365-372 (2003)
Laboratory of Molecular Biophysics
© Photos by Gianluca Battista/Massimiliano Minocri
Xavier Salvatella
Group Leader
ICREA Researcher
Office Tel : +34 93 40 20459
Lab Tel : +34 93 402 04 61
e-mail : xavier.salvatellairbbarcelona.org
Postdoctoral Fellows
Carlos Walter Bertoncini
tel +34 93 40 20460
e-mail: carlos.bertonciniirbbarcelona.org
Marianela Masin
tel +34 93 40 20461
e-mail: marianela.masinirbbarcelona.org
Robert Brynmor Fenwick
tel +34 93 402 0460
e-mail: robert.fenwickirbbarcelona.org
PhD Students
Anna Montaner
tel +34 93 40 20461
e-mail: anna.montanerirbbarcelona.org
Bahareh Eftekharzadeh
tel +34 93 40 20461
e-mail: bahareh.eftekharzadehirbbarcelona.org
Eva De Mol
tel +34 93 40 20461
e-mail: eva.demolirbbarcelona.org
Giulio Chiesa
tel +34 93 40 20461
e-mail: giulio.chiesairbbarcelona.org
Research Assistants
Jordi Silvestre
tel +34 93 40 20461
e-mail: jordi.silvestreirbbarcelona.org
Lab Technicians
Joan Miquel Valverde
tel +34 93 40 20461
e-mail: joan.valverdeirbbarcelona.org
Visiting Scientists
Santiago Esteban
tel +34 93 40 20460
e-mail: santiago.estebanirbbarcelona.org
Laboratory of Molecular Biophysics
- 26 October 2011
Diario Médico
Molecular dynamics may change the research on future drugs - 30 August 2011
Nature Chemistry
Protein dynamics: Whispering within - 28 June 2011
Science News
The dancing amino acids of ubiquitinResearchers at IRB Barcelona have succeeded in following the correlated movements of ubiquitin’s amino acids located far away from one another to transfer information across protein structures.
- 14 June 2011
Science News
The fight against the toxic aggregation of proteins according to DarwinScientists at IRB Barcelona and the BSC discover that some proteins have chemical bonds that prevent the formation of toxic aggregates.
The study sheds light on how proteins have evolved to prevent the cell toxicity associated with toxic aggregates. - 2 June 2011
Investigación y Ciencia
Elusive proteins - 27 April 2011
Barcelona Visió
Kennedy’s Disease, a mystery, but not for much longer - 15 April 2011
Institute News
IRB Barcelona and the BSC renew and expand their joint research programme in order to further computational biologyIRB Barcelona and the BSC show their commitment to computational biology by renewing the Joint IRB-BSC Programme, which also doubles in the number of researchers involved.
The programme aims to position itself as an international leader in computational biology. - 8 March 2011
Chemistry World
Tracking the early stages of Alzheimer’s disease - 24 January 2011
Publico
The inevitable migration toll of scientific research - 21 October 2010
Institute News
IRB Barcelona coordinates a study on rare diseasesXavier Salvatella has been awarded a project by the Fundació La Marató de TV3 funded with 397,000 € to study Kennedy’s disease, a neurodegenerative condition.
The project is coordinated with the Institute of Biomedicine of the University of Barcelona (IBUB) and the University of Cambridge.
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