Módszerek összehasonlítása

	Krio-elektronmikroszkópos rekonstrukció	Homológia modellezés	Molekuláris dokkolás	PPI hálózat topológia
Tudományterület	Bioinformatika	Bioinformatika	Bioinformatika	Bioinformatika
Módszercsalád	Process / pipeline	Process / pipeline	Process / pipeline	Process / pipeline
Keletkezés éve	1975	1993	1982	2000
Megalkotó	Joachim Frank	Andrej Sali	Irwin Kuntz	Peter Uetz
Típus	Image reconstruction pipeline	Comparative structure prediction pipeline	Binding prediction pipeline	Network analysis pipeline
Alapmű	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.
Alternatív nevek	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
Kapcsolódó	3	4	4	3
Összefoglaló	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.