Methoden vergelijken
Bekijk de geselecteerde methoden naast elkaar; rijen die verschillen zijn gemarkeerd.
| HMMER Profiel Zoekopdracht× | Cryo-EM Reconstructie× | |
|---|---|---|
| Vakgebied | Bio-informatica | Bio-informatica |
| Familie | Process / pipeline | Process / pipeline |
| Jaar van ontstaan≠ | 1994 | 1975 |
| Grondlegger≠ | Sean Eddy | Joachim Frank |
| Type≠ | Probabilistic sequence search pipeline | Image reconstruction pipeline |
| Oorspronkelijke bron≠ | 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 ↗ | Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319. DOI ↗ |
| Aliassen | profile-hidden Markov model, HMM profile search, HMMER | cryo-electron microscopy, cryo-EM, single-particle cryo-EM |
| Verwant | 3 | 3 |
| Samenvatting≠ | 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. | 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. |
| ScholarGateGegevensset ↗ |
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