Publications

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Journal Article
Durrieu M.P, Bond P.J, Sansom M.S, Lavery R., Baaden M.  2009.  Coarse-grain simulations of the R-SNARE fusion protein in its membrane environment detect long-lived conformational sub-states. Chemphyschem. 10:1548–1552.
Gabb H., Prévost C, Bertucat G., Robert CH, Lavery R.  1997.  Collective-variable Monte Carlo simulation of DNA. J. Comp. Chem.. 18:2001–2011.
Prévost C, Takahashi M., Lavery R.  2009.  Deforming DNA: from physics to biology. Chemphyschem. 10:1399–404.
Bastard K, Thureau A, Lavery R, Prévost C.  2003.  Docking macromolecules with flexible segments. J. Comput. Chem.. 24:1910–20.
Gabb HA, Lavery R, Prévost C.  1995.  Efficient conformational space sampling for nucleosides using internal coordinate Monte-Carlo simulations and a modified furanose description. J. Comput. Chem.. 16:667–680.
Sacquin-Mora S, Carbone A., Lavery R.  2008.  Identification of Protein Interaction Partners and Protein-Protein Interaction Sites. J. Mol. Biol.. 382:1276–1289.
Sacquin-Mora S, Lavery R.  2006.  Investigating the local flexibility of functional residues in hemoproteins. Biophys. J.. 90:2706–2717.
Sacquin-Mora S, Lavery R..  2009.  Modeling the Mechanical Response of Proteins to Anisotropic Deformation. Chemphyschem. 10:115–118.
Bertucat G, Lavery R, Prévost C.  1998.  A model for parallel triple helix formation by RecA: single-single association with a homologous duplex via the minor groove. J. Biomol. Struct. Dyn.. 16:535–46.
Bertucat G, Lavery R, Prévost C.  1999.  A molecular model for RecA-promoted strand exchange via parallel triple-stranded helices. Biophys. J.. 77:1562–76.
Prévost C, Louise-May S, Ravishanker G, Lavery R, Beveridge DL.  1993.  Persistence analysis of the static and dynamical helix deformations of DNA oligonucleotides: application to the crystal structure and molecular dynamics simulation of d(CGCGAATTCGCG)2. Biopolymers. 33:335–50.
Sacquin-Mora S, Sebban P., Derrien V., Frick B., Lavery R, Alba-Simionesco C..  2007.  Probing the flexibility of the bacterial reaction center: The wild-type protein is more rigid than two site-specific mutants. Biochemistry. 46:14960–14968.