Salīdzināt metodes
Apskatiet izvēlētās metodes blakus; rindas, kas atšķiras, ir izceltas.
| Homoloģijas modelēšana× | Rekonstrukcija ar krioelektronmikroskopiju× | |
|---|---|---|
| Nozare | Bioinformātika | Bioinformātika |
| Saime | Process / pipeline | Process / pipeline |
| Izcelsmes gads≠ | 1993 | 1975 |
| Autors≠ | Andrej Sali | Joachim Frank |
| Tips≠ | Comparative structure prediction pipeline | Image reconstruction pipeline |
| Pirmavots≠ | Sali, A. & Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. Journal of Molecular Biology, 234(3), 779-815. DOI ↗ | Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319. DOI ↗ |
| Citi nosaukumi≠ | comparative modeling, template-based modeling | cryo-electron microscopy, cryo-EM, single-particle cryo-EM |
| Saistītās≠ | 4 | 3 |
| Kopsavilkums≠ | 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. | 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. |
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