Usòrò:Triad chemical mech.png

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Mmẹkụwátá

Nkówá
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.
Ǹgụ́ụ̀bọ̀chị̀
Mkpọlọ́gwụ̀ Thomas, Shafee, (2014). "Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity". PhD Thesis. University of Cambridge.
Odé ákwụ́kwọ́ Thomas Shafee

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depicts Bekee

23 Ọktoba 2013

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dị ùgbu â20:24, 23 Ọktoba 2013NvóÁká màkà otù ȯ dị nà 20:24, 23 Ọktoba 2013566 × 267 (7 KB)Evolution and evolvabilitysmall edit to nucleophile
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