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File:Triad chemical mech.png

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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.
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Tupunga 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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23 ʻOkatopa 2013

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taka20:24, 23 ʻOkatopa 2013ʻAtasiʻi ki he paaki he 20:24, 23 ʻOkatopa 2013566 × 267 (7 KB)Evolution and evolvabilitysmall edit to nucleophile
19:57, 23 ʻOkatopa 2013ʻAtasiʻi ki he paaki he 19:57, 23 ʻOkatopa 2013566 × 267 (7 KB)Evolution and evolvabilitywider
19:50, 23 ʻOkatopa 2013ʻAtasiʻi ki he paaki he 19:50, 23 ʻOkatopa 2013346 × 262 (7 KB)Evolution and evolvabilityUser created page with UploadWizard

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