ᱨᱮᱫ:Triad chemical mech.png

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ᱣᱤᱠᱤᱯᱤᱰᱤᱭᱟ, ᱨᱟᱲᱟ ᱜᱮᱭᱟᱱ ᱯᱩᱛᱷᱤ ᱠᱷᱚᱱ

Triad_chemical_mech.png ‎(᱕᱖᱖ x ᱒᱖᱗ pixels, file size: ᱗ KB, MIME type: image/png)

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ᱢᱩᱬᱩᱛ ᱠᱟᱛᱷᱟ

ᱵᱤᱵᱚᱨᱚᱱᱤ
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.
ᱢᱟᱹᱦᱤᱛ
ᱯᱷᱮᱰᱟᱛ Thomas, Shafee, (2014). "Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity". PhD Thesis. University of Cambridge.
ᱚᱱᱚᱞᱤᱭᱟᱹ Thomas Shafee

ᱞᱟᱭᱥᱮᱱᱥ ᱛᱮᱭᱟᱨ

I, the copyright holder of this work, hereby publish it under the following license:
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ᱟᱲᱟᱜ ᱜᱮᱭᱟᱢ:
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ᱞᱟᱛᱟᱨ ᱨᱮᱭᱟᱜ ᱨᱤᱛ ᱞᱮᱠᱟᱛᱮ:
  • ᱟᱴᱨᱤᱵᱩᱥᱚᱱ – ᱟᱢ ᱠᱟᱹᱢᱤ ᱥᱚᱫᱚᱨ ᱦᱩᱭᱟᱢᱟ ᱡᱚᱠᱷᱚᱱ ᱚᱱᱚᱞᱤᱭᱟᱹ ᱟᱨᱵᱟᱝ ᱞᱟᱭᱥᱮᱸᱥᱩᱭᱟᱹ ᱫᱟᱨᱟᱭᱛᱮ ᱠᱟᱛᱷᱟ ᱨᱟᱠᱟᱵ ᱠᱷᱟᱱ (ᱢᱮᱱᱠᱷᱟᱱ ᱟᱠᱚ ᱩᱫᱩᱜᱟᱜ ᱦᱚᱨ ᱛᱮᱫᱚ ᱵᱟᱝ ᱡᱟᱦᱟᱸ ᱟᱠᱚᱠᱚ ᱜᱚᱲᱚᱣᱟᱢ ᱟᱨᱵᱟᱝ ᱟᱢᱟᱜ ᱠᱟᱹᱢᱤ ᱨᱮᱱᱟᱜ ᱵᱮᱵᱷᱟᱨ)
  • ᱦᱟᱹᱴᱤᱧ ᱱᱚᱝᱠᱟ ᱜᱮ – ᱟᱢ ᱡᱩᱫᱤ ᱠᱟᱹᱢᱤ ᱵᱚᱫᱚᱞ, ᱛᱚᱨᱡᱚᱢᱟ, ᱵᱟᱝᱠᱷᱟᱱ ᱱᱚᱣᱟ ᱠᱟᱹᱢᱤ ᱪᱮᱛᱟᱱᱨᱮ ᱱᱟᱣᱟ ᱠᱟᱹᱢᱤ ᱥᱤᱨᱡᱟᱹᱣᱮᱢ ᱛᱮᱭᱟᱨ ᱠᱷᱟᱱ, ᱛᱚᱵᱮ ᱟᱢ ᱫᱚ ᱚᱱᱟ ᱠᱟᱹᱢᱤ ᱚᱱᱟ ᱢᱤᱫ ᱞᱟᱤᱥᱮᱱᱥ ᱥᱮ ᱚᱱᱟ ᱞᱮᱠᱟᱱᱟᱜ ᱞᱟᱤᱥᱮᱱᱥ ᱨᱮᱜᱮ ᱪᱟᱞ ᱦᱩᱭᱩᱜ ᱛᱟᱢᱟ᱾

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ᱨᱮᱫ ᱨᱮᱭᱟᱜ ᱱᱟᱜᱟᱢ

ᱚᱠᱛᱚ ᱨᱮ ᱞᱤᱱ ᱢᱮ/ᱚᱠᱛᱚ ᱨᱮ ᱨᱮᱫ ᱧᱮᱞ ᱞᱟᱹᱜᱤᱛ ᱞᱤᱱ ᱢᱮ

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ᱱᱚᱸᱰᱮ ᱫᱚ ᱟᱨ ᱮᱴᱟᱜ ᱥᱟᱦᱴᱟᱠᱚ ᱵᱟᱱᱩᱜ-ᱟ ᱡᱟᱸᱦᱟᱸ ᱥᱟᱶᱛᱮ ᱱᱤᱭᱟᱹ ᱨᱮᱫ ᱨᱮᱱᱟᱜ ᱡᱚᱱᱚᱲ ᱢᱮᱱᱟᱜ-ᱟ

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ᱱᱚᱶᱟ ᱨᱮᱫᱠᱚ ᱵᱮᱵᱷᱟᱨᱟᱠᱟᱫ ᱣᱤᱠᱤᱠᱚ :

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