Jämför metoder

	Kryo-EM-rekonstruktion	Homologimodellering	Molekylär dockning
Ämnesområde	Bioinformatik	Bioinformatik	Bioinformatik
Familj	Process / pipeline	Process / pipeline	Process / pipeline
Ursprungsår	1975	1993	1982
Upphovsperson	Joachim Frank	Andrej Sali	Irwin Kuntz
Typ	Image reconstruction pipeline	Comparative structure prediction pipeline	Binding prediction pipeline
Ursprungskälla	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.
Alias	cryo-electron microscopy, cryo-EM, single-particle cryo-EM	comparative modeling, template-based modeling	protein-ligand docking, binding prediction
Närliggande	3	4	4
Sammanfattning	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.