Σύγκριση μεθόδων
Εξετάστε τις επιλεγμένες μεθόδους δίπλα-δίπλα· οι γραμμές που διαφέρουν επισημαίνονται.
| Ανασύσταση με Κρυο-Ηλεκτρονική Μικροσκοπία× | Αναζήτηση Προφίλ HMMER× | |
|---|---|---|
| Πεδίο | Βιοπληροφορική | Βιοπληροφορική |
| Οικογένεια | Process / pipeline | Process / pipeline |
| Έτος προέλευσης≠ | 1975 | 1994 |
| Δημιουργός≠ | Joachim Frank | Sean Eddy |
| Τύπος≠ | Image reconstruction pipeline | Probabilistic sequence search pipeline |
| Θεμελιώδης πηγή≠ | Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319. DOI ↗ | 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. DOI ↗ |
| Εναλλακτικές ονομασίες | cryo-electron microscopy, cryo-EM, single-particle cryo-EM | profile-hidden Markov model, HMM profile search, HMMER |
| Συναφείς | 3 | 3 |
| Σύνοψη≠ | 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. |
| ScholarGateΣύνολο δεδομένων ↗ |
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