Dr Carlo Camilloni

University position

Research Associate


Department of Chemistry



Home page

https://sites.google.com/site/ca... (personal home page)

Research Theme

Systems and Computational Neuroscience


I work on the characterisation of the dynamics of proteins using both atomistic Molecular Dynamics simulations and experimental modelling to unveil the mechanisms at the basis of protein function and misfunction. I am also developing simulation methodologies for enhancing the sampling of the conformational space of complex biomolecules and increasing the quality of the force fields used to describe them.

Research Focus


Molecular Dynamics

Free Energy



Protein Dynamics

Clinical conditions

Alzheimer's disease


Parkinson's disease

Prion diseases


Computational modelling


No collaborators listed

Associated News Items

    Key publications

    Brewer KD, Bacaj T, Cavalli A, Camilloni C, Swarbrick JD, Liu J, Zhou A, Zhou P, Barlow N, Xu J, Seven AB, Prinslow EA, Voleti R, Häussinger D, Bonvin AM, Tomchick DR, Vendruscolo M, Graham B, Südhof TC, Rizo J (2015), “Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution.” Nat Struct Mol Biol 22(7):555-64 Details

    Camilloni C, Sahakyan AB, Holliday MJ, Isern NG, Zhang F, Eisenmesser EZ, Vendruscolo M (2014), “Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism.” Proc Natl Acad Sci U S A 111(28):10203-8 Details

    Camilloni C, Vendruscolo M (2014), “Statistical mechanics of the denatured state of a protein using replica-averaged metadynamics.” J Am Chem Soc 136(25):8982-91 Details

    Gianni S, Camilloni C, Giri R, Toto A, Bonetti D, Morrone A, Sormanni P, Brunori M, Vendruscolo M (2014), “Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein.” Proc Natl Acad Sci U S A 111(39):14141-6 Details

    Camilloni C, De Simone A, Vranken WF, Vendruscolo M (2012), “Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts.” Biochemistry 51(11):2224-31 Details

    Camilloni C, Robustelli P, De Simone A, Cavalli A, Vendruscolo M (2012), “Characterization of the conformational equilibrium between the two major substates of RNase A using NMR chemical shifts.” J Am Chem Soc 134(9):3968-71 Details



    Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M (2015), “89 Constructing free energy landscapes of RNAs at atomic resolution and characterisation of their excited states.” J Biomol Struct Dyn 33 Suppl 1:58 Details

    Camilloni C, Vendruscolo M (2015), “A Tensor-Free Method for the Structural and Dynamical Refinement of Proteins using Residual Dipolar Couplings.” J Phys Chem B 119(3):653-61 Details

    Camilloni C, Vendruscolo M (2015), “Reply to "Comment on 'A Tensor-Free Method for the Structural and Dynamic Refinement of Proteins using Residual Dipolar Couplings'".” J Phys Chem B 119(25):8225-6 Details

    Holliday MJ, Camilloni C, Armstrong GS, Isern NG, Zhang F, Vendruscolo M, Eisenmesser EZ (2015), “Structure and Dynamics of GeoCyp: A Thermophilic Cyclophilin with a Novel Substrate Binding Mechanism That Functions Efficiently at Low Temperatures.” Biochemistry Details

    Kukic P, Alvin Leung HT, Bemporad F, Aprile FA, Kumita JR, De Simone A, Camilloni C, Vendruscolo M (2015), “Structure and Dynamics of the Integrin LFA-1 I-Domain in the Inactive State Underlie its Inside-Out/Outside-In Signaling and Allosteric Mechanisms.” Structure 23(4):745-53 Details

    Porcari R, Proukakis C, Waudby CA, Bolognesi B, Mangione PP, Paton JF, Mullin S, Cabrita LD, Penco A, Relini A, Verona G, Vendruscolo M, Stoppini M, Tartaglia GG, Camilloni C, Christodoulou J, Schapira AH, Bellotti V (2015), “The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein.” J Biol Chem 290(4):2395-404 Details

    Sormanni P, Camilloni C, Fariselli P, Vendruscolo M (2015), “The s2D method: simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins.” J Mol Biol 427(4):982-96 Details


    Blombach F, Launay H, Snijders AP, Zorraquino V, Wu H, de Koning B, Brouns SJ, Ettema TJ, Camilloni C, Cavalli A, Vendruscolo M, Dickman MJ, Cabrita LD, La Teana A, Benelli D, Londei P, Christodoulou J, van der Oost J (2014), “Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain.” Biochem J 462(2):373-84 Details

    Fu B, Sahakyan AB, Camilloni C, Tartaglia GG, Paci E, Caflisch A, Vendruscolo M, Cavalli A (2014), “ALMOST: an all atom molecular simulation toolkit for protein structure determination.” J Comput Chem 35(14):1101-5 Details

    Kannan A, Camilloni C, Sahakyan AB, Cavalli A, Vendruscolo M (2014), “A Conformational Ensemble Derived Using NMR Methyl Chemical Shifts Reveals a Mechanical Clamping Transition That Gates the Binding of the HU Protein to DNA.” J Am Chem Soc 136(6):2204-7 Details

    Kendrick AA, Holliday MJ, Isern NG, Zhang F, Camilloni C, Huynh C, Vendruscolo M, Armstrong G, Eisenmesser EZ (2014), “The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide.” Protein Sci 23(4):464-80 Details

    Krieger JM, Fusco G, Lewitzky M, Simister PC, Marchant J, Camilloni C, Feller SM, De Simone A (2014), “Conformational recognition of an intrinsically disordered protein.” Biophys J 106(8):1771-9 Details

    Kukic P, Camilloni C, Cavalli A, Vendruscolo M (2014), “Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.” J Mol Biol 426(8):1826-38 Details

    Leung HT, Kukic P, Camilloni C, Bemporad F, De Simone A, Aprile FA, Kumita JR, Vendruscolo M (2014), “NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain.” Protein Sci 23(11):1596-606 Details

    Montalvao R, Camilloni C, De Simone A, Vendruscolo M (2014), “New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics.” J Biomol NMR 58(4):233-8 Details


    Camilloni C, Cavalli A, Vendruscolo M (2013), “Assessment of the use of NMR chemical shifts as replica-averaged structural restraints in molecular dynamics simulations to characterize the dynamics of proteins.” J Phys Chem B 117(6):1838-43 Details

    Camilloni C, Vendruscolo M (2013), “A relationship between the aggregation rates of α-synuclein variants and the β-sheet populations in their monomeric forms.” J Phys Chem B 117(37):10737-41 Details

    Cavalli A, Camilloni C, Vendruscolo M (2013), “Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle.” J Chem Phys 138(9):094112 Details

    Granata D, Camilloni C, Vendruscolo M, Laio A (2013), “Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.” Proc Natl Acad Sci U S A 110(17):6817-22 Details

    Waudby CA, Camilloni C, Fitzpatrick AW, Cabrita LD, Dobson CM, Vendruscolo M, Christodoulou J (2013), “In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells.” PLoS One 8(8):e72286 Details


    Camilloni C, Schaal D, Schweimer K, Schwarzinger S, De Simone A (2012), “Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.” Biophys J 102(1):158-67 Details

    Heidarsson PO, Valpapuram I, Camilloni C, Imparato A, Tiana G, Poulsen FM, Kragelund BB, Cecconi C (2012), “A Highly Compliant Protein Native State with a Spontaneous-like Mechanical Unfolding Pathway.” J Am Chem Soc 134(41):17068-75 Details

    Sutto L, Camilloni C (2012), “From A to B: A ride in the free energy surfaces of protein G domains suggests how new folds arise.” J Chem Phys 136(18):185101 Details

    Tiana G, Camilloni C (2012), “Ratcheted molecular-dynamics simulations identify efficiently the transition state of protein folding.” J Chem Phys 137(23):235101 Details


    Camilloni C, Broglia RA, Tiana G (2011), “Hierarchy of folding and unfolding events of protein G, CI2, and ACBP from explicit-solvent simulations.” J Chem Phys 134(4):045105 Details


    Caldarini M, Sutto L, Camilloni C, Vasile F, Broglia RA, Tiana G (2009), “Identification of the folding inhibitors of hen-egg lysozyme: gathering the right tools.” Eur Biophys J Details

    Camilloni C, Sutto L (2009), “Lymphotactin: how a protein can adopt two folds.” J Chem Phys 131(24):245105 Details


    Calosci N, Chi CN, Richter B, Camilloni C, Engström A, Eklund L, Travaglini-Allocatelli C, Gianni S, Vendruscolo M, Jemth P (2008), “Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins.” Proc Natl Acad Sci U S A 105(49):19241-6 Details

    Camilloni C, Provasi D, Tiana G, Broglia RA (2008), “Exploring the protein G helix free-energy surface by solute tempering metadynamics.” Proteins 71(4):1647-54 Details

    Camilloni C, Rocco AG, Eberini I, Gianazza E, Broglia RA, Tiana G (2008), “Urea and guanidinium chloride denature protein L in different ways in molecular dynamics simulations.” Biophys J 94(12):4654-61 Details

    Camilloni C, Sutto L, Provasi D, Tiana G, Broglia RA (2008), “Early events in protein folding: Is there something more than hydrophobic burst?” Protein Sci 17(8):1424-33 Details

    Marini F, Camilloni C, Provasi D, Broglia RA, Tiana G (2008), “Metadynamic sampling of the free-energy landscapes of proteins coupled with a Monte Carlo algorithm.” Gene 422(1-2):37-40 Details

    Verkhivker G, Tiana G, Camilloni C, Provasi D, Broglia RA (2008), “Atomistic simulations of the HIV-1 protease folding inhibition.” Biophys J 95(2):550-62 Details


    Camilloni C, Provasi D, Tiana G, Broglia RA (2007), “Optical absorption of a green fluorescent protein variant: environment effects in a density functional study.” J Phys Chem B 111(36):10807-12 Details