File:Triad chemical mech.png
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བསྡུས་དོན།
| 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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ཟླ་ཚེས་/དུས་ཚོད་གནུན་ཏེ་རྩོམ་ཡིག་ལ་ལྟ་བ།
| ཚེས་གྲངས། / དུས་ཚོད། | བསྡུས་དོན། | ཚད། | སྤྱོད་མི། | བསམ་ཚུལ། | |
|---|---|---|---|---|---|
| ད་ལྟ། | ༢༠:༢༤, ༢༣ ཟླ་བཅུ་བ། ༢༠༡༣ | | ༥༦༦ × ༢༦༧ (༧ KB) | Evolution and evolvability | small edit to nucleophile |
| ༡༩:༥༧, ༢༣ ཟླ་བཅུ་བ། ༢༠༡༣ |  | ༥༦༦ × ༢༦༧ (༧ KB) | Evolution and evolvability | wider | |
| ༡༩:༥༠, ༢༣ ཟླ་བཅུ་བ། ༢༠༡༣ |  | ༣༤༦ × ༢༦༢ (༧ KB) | Evolution and evolvability | User created page with UploadWizard |
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