tóng-àn:Serpin equilibrium.png
Seng khoàⁿ chiàm-liōng: 800 × 507 siōng-sò͘. Kî-thaⁿ--ê kái-sek-tō͘: 320 × 203 siōng-sò͘ | 640 × 406 siōng-sò͘ | 1,024 × 649 siōng-sò͘ | 1,280 × 812 siōng-sò͘ | 3,000 × 1,902 siōng-sò͘.
Choân kái-sek-tō͘ （3,000 × 1,902 siōng-sò͘ , tóng-àn chiàm-liōng: 1.41 MB, MIME luī-hêng: image/png）
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Khài-iàu
| Soat-bêng |
English: The native state of serpins is an equilibrium between a fully-stressed state (left) and a partially relaxed state (right). The five-stranded A-sheet (light blue) contains two functionally important regions for the serpin's mechanism, the breach and the shutter. The Reactive Centre Loop (RCL, blue) exists in a dynamic equilibrium between the fully exposed conformation (left) and a conformation where it is partially inserted into the breach of the A-sheet (right). (PDB: 1QLP, 1YXA).
[1] [2] |
| Ji̍t-kî | |
| Chhut-chhù | Ka-tī chò--ê |
| Chok-chiá | Thomas Shafee |
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- ↑ Elliott PR, Lomas DA, Carrell RW, Abrahams JP. (1996). "Inhibitory conformation of the reactive loop of alpha 1-antitrypsin". Nature Structural & Molecular Biology 3 (8): 676–81. DOI:10.1038/nsb0896-676. PMID 8756325.
- ↑ (2005). "The murine orthologue of human antichymotrypsin: a structural paradigm for clade A3 serpins.". J Biol Chem 280 (52): 43168–78. DOI:10.1074/jbc.M505598200. PMID 16141197.
Tóng-àn le̍k-sú
Chhi̍h ji̍t-kî/sî-kan, khoàⁿ hit sî-chūn--ê tóng-àn.
| Ji̍t-kî/Sî-kan | 細張圖 | 寸尺 | Iōng-chiá | Chù-kái | |
|---|---|---|---|---|---|
| hiān-chāi | 2016-nî 10-goe̍h 6-ji̍t (pài-sì) 23:23 | | 3,000 × 1,902（1.41 MB） | Cmdrjameson | Compressed with pngout. Reduced by 772kB (34% decrease). |
| 2016-nî 3-goe̍h 19-ji̍t (pài-la̍k) 23:05 |  | 3,000 × 1,902（2.16 MB） | Evolution and evolvability | Colour tweaks | |
| 2015-nî 12-goe̍h 14-ji̍t (pài-it) 12:05 |  | 1,246 × 765（476 KB） | Evolution and evolvability | Cross-wiki upload from en.wikipedia.org |
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