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Summary
| Description |
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. |
| Date | |
| Source | Thomas, Shafee, (2014). "Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity". PhD Thesis. University of Cambridge. |
| Author | Thomas Shafee |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 20:24, 23 October 2013 | | 566 × 267 (7 KB) | Evolution and evolvability | small edit to nucleophile |
| 19:57, 23 October 2013 |  | 566 × 267 (7 KB) | Evolution and evolvability | wider | |
| 19:50, 23 October 2013 |  | 346 × 262 (7 KB) | Evolution and evolvability | User created page with UploadWizard |
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