Publications

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Sacquin-Mora S.  2015.  Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus? J. R. Soc. Interface. 12
Sacquin-Mora S.  2003.  Fluide nanoconfines dans des systemes de basse symetrie : Simulations et Theorie.
Sacquin-Mora S, Prévost C.  2021.  When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes. Biomolecules. 11:1529.
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.
Sacquin-Mora S, Schoen M., Fuchs A.H.  2002.  Fluids confined by nanopatterned substrates of low symmetry. Mol. Phys.. 100:2971–2982.
Sacquin-Mora S, Delalande O., Baaden M.  2010.  Functional Modes and Residue Flexibility Control the Anisotropic Response of Guanylate Kinase to Mechanical Stress. Biophys. J.. 99:3412–3419.
Sacquin-Mora S, Lavery R..  2009.  Modeling the Mechanical Response of Proteins to Anisotropic Deformation. Chemphyschem. 10:115–118.
Sacquin-Mora S, Fuchs AH, Schoen M.  2004.  Torsion-induced phase transitions in fluids confined between chemically decorated substrates. J. Chem. Phys.. 121:9077–9086.
Sacquin-Mora S, Laforet E, Lavery R.  2007.  Locating the active sites of enzymes using mechanical properties. Proteins: Struct., Funct., Bioinf.. 67:350–359.
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Russo P., Taly A.  2012.  α7-Nicotinic acetylcholine receptors: an old actor for new different roles. Curr. Drug Targets. 13:574–578.
Roth CA, Dreyfus T, Robert CH, Cazals F.  2016.  Hybridizing Rapidly Exploring Random Trees and Basin Hopping Yields an Improved Exploration of Energy Landscapes. J. Comput. Chem.. 37:752.
Röper J-C, Mitrossilis D, Stirnemann G, Waharte F, Brito I, Fernandez-Sanchez M-E, Baaden M, Salamero J, Farge E.  2018.  The major β-catenin/E-cadherin junctional binding site is a primary molecular mechano-transductor of differentiation .. Elife. 7
Röder K, Stirnemann G, Dock-Bregeon A-C, Wales DJ, Pasquali S.  2020.  Structural transitions in the RNA 7SK 5' hairpin and their effect on HEXIM binding. Nucleic Acids Res. 48:373-389.
Robert CH, Janin J.  1998.  A soft, mean–field potential derived from crystal contacts for predicting protein–protein interactions. J. Mol. Biol.. 283:1037–1047.
Robert CH, Gill SJ, Wyman J.  1988.  Quantitative analysis of linkage in macromolecules when one ligand is present in limited total quantity. Biochemistry. 27:6829–6835.
Robert CH, Ho PS.  1995.  Significance of bound water to local chain conformations in protein crystals. Proc. Natl. Acad. Sci. U.s.a.. 92:7600–7604.
Robert CH, Fall L, Gill SJ.  1988.  Linkage of organic phosphates to oxygen binding in human hemoglobin at high concentrations. Biochemistry. 27:6835–6843.
Robert CH, Cherfils J, Mouawad L, Perahia D.  2004.  Integrating three views of Arf1 activation dynamics. J. Mol. Biol.. 337:969–983.
Robert CH, Decker H, Richey B, Gill SJ, Wyman J.  1987.  Nesting: hierarchies of allosteric interactions. Proc. Natl. Acad. Sci. U.s.a.. 84:1891–1895.
Robert CH.  1990.  A hierarchical `nesting' approach to describe the stability of alpha helices with side-chain interactions. Biopolymers. 30:335–347.
Robert CH.  1995.  Estimating friction coefficients of mixed globular/chain molecules, such as protein/DNA complexes. Biophys. J.. 69:840–848.
Robert CH, Colosimo A, Gill SJ.  1989.  Allosteric formulation of thermal transitions in macromolecules, including effects of ligand binding and oligomerization. Biopolymers. 28:1705–1729.
Riccardi L, Nguyen PHoang, Stock G.  2009.  Free-Energy Landscape of RNA Hairpins Constructed via Dihedral Angle Principal Component Analysis. J. Phys. Chem. B. 113:16660–16668.
Reddy T., Shorthouse D., Parton D.L, Jefferys E., Fowler P.W, Chavent M, Baaden M, Sansom M.S.  2015.  Nothing to sneeze at: a dynamic and integrative computational model of an influenza A virion. Structure. 23:584–597.
Rahaman O., Kalimeri M., Katava M., Paciaroni A., Sterpone F..  2017.  Configurational Disorder of Water Hydrogen Bond Network at the Protein Dynamical Transition. J. Phys. Chem. B. 121:6792−6798.

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