Ymele:Serpin mechanism.png
Micelness þisre forebysene: 725 be 599 dotta. Oðra metinga brædo: 290 be 240 dotta | 581 be 480 dotta | 929 be 768 dotta | 1,239 be 1,024 dotta | 1,800 be 1,488 dotta.
Frumlicu ymele (1,800 × 1,488 pixela, ymelan micelness: 513 KB, MIME cynn: image/png)
Scortness
| Towritenness |
English: Serine proteases operate by a two-step catalytic mechanism. First, the substrate (blue) is attacked by the catalytic triad (red) to form an acyl-enzyme intermediate. The intermediate is typically resolved by hydrolysis by water. However, when the reactive centre loop (RCL) of a serpin is attacked, the conformational change (blue arrow) pulls the catalytic triad out of position, preventing it from completing catalysis. (Based on PDB: 1K9O, 1EZX) |
| Tælmearc | |
| Fruma | Agen weorc |
| Dædfruma | Thomas Shafee |
Leaf:
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- Þu most:
- bryttian – to copy, distribute and transmit the work
- to remix – andwendan þæt weorc
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Ymelan stær
Swing dæg/tide mid mys to seonne þa ymelan swa heo wæs on þære tide geywed.
| Dæg/Tid | Metungincel | Micelnesse gemetu | Brucend | Ymbspræc | |
|---|---|---|---|---|---|
| nu | 09:56, 22 Gēolmōnaþ 2015 | | 1,800 × 1,488 (513 KB) | Evolution and evolvability | Higher resolution |
| 05:19, 19 Gēolmōnaþ 2015 |  | 1,362 × 1,126 (300 KB) | Evolution and evolvability | Minor arrow correction | |
| 05:08, 19 Gēolmōnaþ 2015 |  | 1,362 × 1,126 (300 KB) | Evolution and evolvability | added arrow and removed transparency | |
| 05:04, 19 Gēolmōnaþ 2015 |  | 1,362 × 1,114 (360 KB) | Evolution and evolvability | Cross-wiki upload from en.wikipedia.org |
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