Fasciculus:Triad chemical mech.png
Nulla maior resolutio exstat.
Triad_chemical_mech.png (566 × 267 elementa imaginalia, magnitudo fasciculi: 7 chiliocteti, typus MIME: image/png)
Summarium
| Descriptio |
English: A catalytic triad charge-relay system as commonly found in proteases. The acid residue (commonly glutamate or aspartate) aligns and polarises the base (usually histidine) which activates the nucleophile (often serine or cysteine, occasionally threonine). The catalytic triad reduces the pKa of the nucleophilic residue which then performs a nucleophilic attack on the substrate. |
| Datum | |
| Fons | Thomas, Shafee, (2014). "Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity". PhD Thesis. University of Cambridge. |
| Auctor | Thomas Shafee |
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Historia fasciculi
Presso die vel tempore fasciculum videbis, sicut tunc temporis apparuit.
| Dies/Tempus | Minutio | Dimensiones | Usor | Sententia | |
|---|---|---|---|---|---|
| recentissima | 20:24, 23 Octobris 2013 | | 566 × 267 (7 chiliocteti) | Evolution and evolvability | small edit to nucleophile |
| 19:57, 23 Octobris 2013 |  | 566 × 267 (7 chiliocteti) | Evolution and evolvability | wider | |
| 19:50, 23 Octobris 2013 |  | 346 × 262 (7 chiliocteti) | Evolution and evolvability | User created page with UploadWizard |
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