Сравнение на методи

	Топология на мрежи от протеин-протеинни взаимодействия (PPI)	Реконструкция чрез крио-ЕМ	Молекулярно докиране
Област	Биоинформатика	Биоинформатика	Биоинформатика
Семейство	Process / pipeline	Process / pipeline	Process / pipeline
Година на възникване	2000	1975	1982
Създател	Peter Uetz	Joachim Frank	Irwin Kuntz
Тип	Network analysis pipeline	Image reconstruction pipeline	Binding prediction pipeline
Основополагащ източник	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.	Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319.	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.
Други названия	protein interaction networks, interactome analysis, network topology	cryo-electron microscopy, cryo-EM, single-particle cryo-EM	protein-ligand docking, binding prediction
Свързани	3	3	4
Резюме	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.	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.	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.