@article {2011|1848,
	title = {Free energy profiles along consensus normal modes provide insight into {HIV}-1 protease flap opening},
	journal = {J. Chem. Theor. Comput.},
	volume = {7},
	year = {2011},
	pages = {2348{\textendash}52},
	author = {Paulo R. Batista and Gaurav Pandey and Paulo M. Bisch and Paulo G. Pascutti and David Perahia and Charles H. Robert}
}
@inbook {2011|1417,
	title = {Receptor Flexibility in Ligand Docking and Virtual Screening.},
	booktitle = {In-silico lead discovery},
	year = {2011},
	publisher = {Bentham Science Publishers},
	organization = {Bentham Science Publishers},
	author = {Maria A. Miteva and Charles H. Robert and J. D. Marechal and David Perahia}
}
@article {2006|1810,
	title = {Normal mode analysis as a prerequisite for drug design: Application to matrix metalloproteinases inhibitors},
	journal = {Febs Lett.},
	volume = {580},
	number = {22},
	year = {2006},
	month = {oct},
	pages = {5130{\textendash}5136},
	abstract = {We demonstrate the utility of normal mode analysis in correctly predicting the binding modes of inhibitors in the active sites of matrix metalloproteinases (MMPs). We show the accuracy in predicting the positions of MMP-3 inhibitors is strongly dependent on which structure is used as the target, especially when it has been energy minimized. This dependency can be overcome by using intermediate structures generated along one of the normal modes previously calculated for a given target. These results may be of prime importance for further in silico drug discovery.},
	doi = {10.1016/j.febslet.2006.08.037},
	author = {Nicolas Floquet and Jean-Didier Mar{\'e}chal and Marie-Ange Badet-Denisot and Charles H Robert and Manuel Dauchez and David Perahia}
}
@article {2006|1658,
	title = {Odorant Binding and Conformational Dynamics in the Odorant-binding Protein},
	journal = {J. Biol. Chem.},
	volume = {281},
	number = {40},
	year = {2006},
	month = {oct},
	pages = {29929{\textendash}29937},
	abstract = {In mammals, the olfactory epithelium secretes odorant-binding proteins (OBPs), which are lipocalins found freely dissolved in the mucus layer protecting the olfactory neurons. OBPs may act as passive transporters of predominantly hydrophobic odorant molecules across the aqueous mucus layer, or they may play a more active role in which the olfactory neuronal receptor recognizes the OBP-ligand complex. To better understand the molecular events accompanying the initial steps in the olfaction process, we have performed molecular dynamics studies of rat and pig OBPs with the odorant molecule thymol. These calculations provide an atomic level description of conformational changes and pathway intermediates that remain difficult to study directly. A series of eight independent molecular dynamics trajectories of rat OBP permitted the observation of a consensus pathway for ligand unbinding and the calculation of the potential of mean force (PMF) along this path. Titration microcalorimetry confirmed the specific binding of thymol to this protein with a strong hydrophobic component. In both rat and pig OBPs we observed lipocalin strand pair opening in the presence of ligand, consistent with potential roles of these proteins in olfactive receptor recognition.},
	doi = {10.1074/jbc.M604869200},
	author = {Eric Hajjar and David Perahia and Helene D{\'e}bat and Claude Nespoulous and Charles H. Robert}
}
