Comparer des méthodes

	Reconstruction par cryo-ME	Modélisation par homologie	Dockage moléculaire	Topologie de réseau d'interactions protéine-protéine
Domaine	Bio-informatique	Bio-informatique	Bio-informatique	Bio-informatique
Famille	Process / pipeline	Process / pipeline	Process / pipeline	Process / pipeline
Année d'origine	1975	1993	1982	2000
Auteur d'origine	Joachim Frank	Andrej Sali	Irwin Kuntz	Peter Uetz
Type	Image reconstruction pipeline	Comparative structure prediction pipeline	Binding prediction pipeline	Network analysis pipeline
Source fondatrice	Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319.	Sali, A. & Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. Journal of Molecular Biology, 234(3), 779-815.	Kuntz, I. D., Blaney, J. M., Oatley, S. J., Langridge, R., & Ferrin, T. E. (1982). A geometric approach to macromolecule-ligand interactions. Journal of Molecular Biology, 161(2), 269-288.	Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., ... & Lomax, J. (2000). A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature, 403(6770), 623-627.
Alias	cryo-electron microscopy, cryo-EM, single-particle cryo-EM	comparative modeling, template-based modeling	protein-ligand docking, binding prediction	protein interaction networks, interactome analysis, network topology
Apparentées	3	4	4	3
Résumé	Cryo-electron microscopy (cryo-EM) determines three-dimensional macromolecular structures at atomic or near-atomic resolution by imaging proteins frozen in vitreous ice. Pioneered by Frank, Henderson, and others, this technique has revolutionized structural biology by enabling visualization of large, non-crystallizable complexes and capturing functional conformational states.	Homology modeling, also called comparative modeling, predicts the three-dimensional structure of a protein using an experimentally-solved structure of a homologous protein as a template. Introduced by Sali and Blundell in 1993, this method exploits the principle that homologous proteins share similar spatial structures despite differing in amino acid sequence.	Molecular docking predicts the preferred binding orientation and affinity of a ligand (small molecule) within a protein binding pocket. Pioneered by Kuntz and colleagues in 1982, this computational method searches conformational space to find energetically favorable ligand-protein complexes, enabling rapid screening of chemical libraries for drug discovery.	Protein-protein interaction network analysis identifies and characterizes the structural properties of cellular interaction networks. Pioneered by Uetz and colleagues through large-scale yeast two-hybrid screening, this approach reveals topological features like hubs, modules, and motifs that encode functional organization and disease associations.