Sammenlign metoder

	Kryo-EM Rekonstruktion	Homologymodellering	Molekylær docking
Fagområde	Bioinformatik	Bioinformatik	Bioinformatik
Familie	Process / pipeline	Process / pipeline	Process / pipeline
Oprindelsesår	1975	1993	1982
Ophavsperson	Joachim Frank	Andrej Sali	Irwin Kuntz
Type	Image reconstruction pipeline	Comparative structure prediction pipeline	Binding prediction pipeline
Oprindelig kilde	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.
Aliasser	cryo-electron microscopy, cryo-EM, single-particle cryo-EM	comparative modeling, template-based modeling	protein-ligand docking, binding prediction
Relaterede	3	4	4
Resumé	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.