W. R. Taylor, The classification of amino acid conservation, Journal of Theoretical Biology, vol.119, issue.2, pp.205-218, 1986.
DOI : 10.1016/S0022-5193(86)80075-3

R. Bhattacharyya, D. Pal, and P. Chakrabarti, Disulfide bonds, their stereospecific environment and conservation in protein structures, Protein Engineering Design and Selection, vol.17, issue.11, pp.795-808, 2004.
DOI : 10.1093/protein/gzh093

M. S. Weiss, M. Brandl, J. Suhnel, D. Pal, and R. Hilgenfeld, More hydrogen bonds for the (structural) biologist, Trends in Biochemical Sciences, vol.26, issue.9, pp.521-523, 2001.
DOI : 10.1016/S0968-0004(01)01935-1

W. Kabsch and C. Sander, Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features, Biopolymers, vol.33, issue.12, pp.2577-2637, 1983.
DOI : 10.1002/bip.360221211

R. P. Joosten, T. A. Te-beek, E. Krieger, M. L. Hekkelman, R. W. Hooft et al., A series of PDB related databases for everyday needs, Nucleic Acids Research, vol.39, issue.Database, pp.411-419
DOI : 10.1093/nar/gkq1105

D. Frishman and P. Argos, Knowledge-based protein secondary structure assignment, Proteins: Structure, Function, and Genetics, vol.206, issue.4, pp.566-579, 1995.
DOI : 10.1002/prot.340230412

M. Heinig and D. Frishman, STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins, Nucleic Acids Research, vol.32, issue.Web Server, pp.500-502, 2004.
DOI : 10.1093/nar/gkh429

J. Esque, C. Oguey, and A. G. De-brevern, A Novel Evaluation of Residue and Protein Volumes by Means of Laguerre Tessellation, Journal of Chemical Information and Modeling, vol.50, issue.5, pp.947-960, 2010.
DOI : 10.1021/ci9004892

URL : https://hal.archives-ouvertes.fr/inserm-00473943

A. Poupon, Voronoi and Voronoi-related tessellations in studies of protein structure and interaction, Current Opinion in Structural Biology, vol.14, issue.2, pp.233-241, 2004.
DOI : 10.1016/j.sbi.2004.03.010

J. Ismer, A. S. Rose, J. K. Tiemann, A. Goede, K. Rother et al., Voronoia4RNA--a database of atomic packing densities of RNA structures and their complexes, Nucleic Acids Research, vol.41, issue.D1, pp.280-284, 2012.
DOI : 10.1093/nar/gks1061

S. Mahdavi, A. Mohades, A. Salehzadeh-yazdi, S. Jahandideh, and A. Masoudi-nejad, Computational analysis of RNA???protein interaction interfaces via the Voronoi diagram, Journal of Theoretical Biology, vol.293, pp.55-64, 2012.
DOI : 10.1016/j.jtbi.2011.09.033

K. Nadassy, I. Tomas-oliveira, I. Alberts, J. Janin, and S. J. Wodak, Standard atomic volumes in double-stranded DNA and packing in protein-DNA interfaces, Nucleic Acids Research, vol.29, issue.16, pp.3362-3376, 2001.
DOI : 10.1093/nar/29.16.3362

N. Echols, D. Milburn, and M. Gerstein, MolMovDB: analysis and visualization of conformational change and structural flexibility, Nucleic Acids Research, vol.31, issue.1, pp.478-482, 2003.
DOI : 10.1093/nar/gkg104

F. Birzele, J. E. Gewehr, G. Csaba, and R. Zimmer, Vorolign--fast structural alignment using Voronoi contacts, Bioinformatics, vol.23, issue.2, pp.205-211, 2007.
DOI : 10.1093/bioinformatics/btl294

M. Petrek, P. Kosinova, J. Koca, and M. Otyepka, MOLE: A Voronoi Diagram-Based Explorer of Molecular Channels, Pores, and Tunnels, Structure, vol.15, issue.11, pp.1357-1363, 2007.
DOI : 10.1016/j.str.2007.10.007

K. Berka, O. Hanak, D. Sehnal, P. Banas, V. Navratilova et al., MOLEonline 2.0: interactive web-based analysis of biomacromolecular channels, Nucleic Acids Research, vol.40, issue.W1, pp.222-227, 2012.
DOI : 10.1093/nar/gks363

J. Bernauer, R. P. Bahadur, F. Rodier, J. Janin, and A. Poupon, DiMoVo: a Voronoi tessellation-based method for discriminating crystallographic and biological protein-protein interactions, Bioinformatics, vol.24, issue.5, pp.652-658, 2008.
DOI : 10.1093/bioinformatics/btn022

URL : https://hal.archives-ouvertes.fr/inria-00431696

G. Faure, A. Bornot, and A. G. De-brevern, Protein contacts, inter-residue interactions and side-chain modelling, Biochimie, vol.90, issue.4, pp.626-639, 2008.
DOI : 10.1016/j.biochi.2007.11.007

URL : https://hal.archives-ouvertes.fr/inserm-00189828

J. C. Gelly and A. G. De-brevern, Protein Peeling 3D: new tools for analyzing protein structures, Bioinformatics, vol.27, issue.1, pp.132-133, 2011.
DOI : 10.1093/bioinformatics/btq610

URL : https://hal.archives-ouvertes.fr/inserm-00568165

J. C. Gelly, A. G. De-brevern, and S. Hazout, 'Protein Peeling': an approach for splitting a 3D protein structure into compact fragments, Bioinformatics, vol.22, issue.2, pp.129-133, 2006.
DOI : 10.1093/bioinformatics/bti773

URL : https://hal.archives-ouvertes.fr/inserm-00133725

J. C. Gelly, C. Etchebest, S. Hazout, and A. G. De-brevern, Protein Peeling 2: a web server to convert protein structures into series of protein units, Nucleic Acids Research, vol.34, issue.Web Server, pp.75-78, 2006.
DOI : 10.1093/nar/gkl292

URL : https://hal.archives-ouvertes.fr/inserm-00133731

J. Esque, C. Oguey, and A. G. De-brevern, Comparative Analysis of Threshold and Tessellation Methods for Determining Protein Contacts, Journal of Chemical Information and Modeling, vol.51, issue.2, pp.493-507, 2011.
DOI : 10.1021/ci100195t

URL : https://hal.archives-ouvertes.fr/inserm-00568174

J. H. Gutow, Easy Jmol Web Pages Using the Jmol Export to Web Function: A Tool for Creating Interactive Web-Based Instructional Resources and Student Projects with Live 3-D Images of Molecules without Writing Computer Code, Journal of Chemical Education, vol.87, issue.6, pp.652-653, 2010.
DOI : 10.1021/ed100283v

H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat et al., The Protein Data Bank, Nucleic Acids Research, vol.28, issue.1, pp.235-242, 2000.
DOI : 10.1093/nar/28.1.235

B. Hess, C. Kutzner, D. Van-der-spoel, and E. Lindahl, GROMACS 4:?? Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation, Journal of Chemical Theory and Computation, vol.4, issue.3, pp.435-447, 2008.
DOI : 10.1021/ct700301q

H. Grubmuller, B. Heymann, and P. Tavan, Ligand Binding: Molecular Mechanics Calculation of the Streptavidin-Biotin Rupture Force, Science, vol.271, issue.5251, pp.997-999, 1996.
DOI : 10.1126/science.271.5251.997

J. Tsai, R. Taylor, C. Chothia, and M. Gerstein, The packing density in proteins: standard radii and volumes, Journal of Molecular Biology, vol.290, issue.1, pp.253-266, 1999.
DOI : 10.1006/jmbi.1999.2829

H. Wang, D. Boisvert, K. K. Kim, R. Kim, and S. H. Kim, Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution, The EMBO Journal, vol.19, issue.3, pp.317-323, 2000.
DOI : 10.1093/emboj/19.3.317

J. F. Sadoc, R. Jullien, and N. Rivier, The Laguerre polyhedral decomposition: application to protein folds, The European Physical Journal B - Condensed Matter, vol.33, issue.3, pp.355-363, 2003.
DOI : 10.1140/epjb/e2003-00176-5