방법 비교

	PPI 네트워크 토폴로지	극저온 전자 현미경 재구성	HMMER 프로파일 검색	분자 도킹
분야	생물정보학	생물정보학	생물정보학	생물정보학
계열	Process / pipeline	Process / pipeline	Process / pipeline	Process / pipeline
기원 연도	2000	1975	1994	1982
창시자	Peter Uetz	Joachim Frank	Sean Eddy	Irwin Kuntz
유형	Network analysis pipeline	Image reconstruction pipeline	Probabilistic sequence search pipeline	Binding prediction pipeline
원전	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.	Krogh, A., Brown, M., Mian, I. S., Sjölander, K., & Haussler, D. (1994). Hidden Markov models in computational biology: applications to protein modeling. Journal of Molecular Biology, 235(5), 1501-1531.	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.
별칭	protein interaction networks, interactome analysis, network topology	cryo-electron microscopy, cryo-EM, single-particle cryo-EM	profile-hidden Markov model, HMM profile search, HMMER	protein-ligand docking, binding prediction
관련	3	3	3	4
요약	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.	HMMER profile search identifies distant protein sequence homologs using probabilistic models of protein families, known as profile Hidden Markov Models (HMMs). Developed by Eddy and colleagues, this method captures sequence variation patterns within protein families and detects homologs with far greater sensitivity than position-weight matrices or pairwise alignment.	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.