Sandbox 11: Difference between revisions
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{{STRUCTURE_2oua | PDB=2oua | SCENE= }} | {{STRUCTURE_2oua | PDB=2oua | SCENE= }} | ||
''Nocardiopsis alba'' Protease A, or NAPase, is an acid-resistant homolog of α-lytic protease (αlp). As such, NAPase and αlp are both kinetically stable proteases, meaning it is the large barrier to unfolding that keeps these proteases in their folded, active state. This is different from most other proteins, which stay in their folded, or native, state because of the energy difference between their native and unfolded states, with the native state being lower in energy. These proteases gain a significant advantage in half-life because of their kinetic stability, but | ''Nocardiopsis alba'' Protease A, or NAPase, is an acid-resistant homolog of α-lytic protease (αlp). As such, NAPase and αlp are both kinetically stable proteases, meaning it is the large barrier to unfolding that keeps these proteases in their folded, active state. This is different from most other proteins, which stay in their folded, or native, state because of the energy difference between their native and unfolded states, with the native state being lower in energy. These proteases gain a significant advantage in half-life to unfolding because of their kinetic stability, but the advantage comes with a price. The barrier to folding is large, with αlp's half life for folding around 1800 years. Luckily, these proteases have coevolved a pro region that can assist with folding while covalently attached, or while in solution with the unfolded protease. Once the protease has been guided to its native state by the pro region, it mercilessly proteolyzes the pro region that helped it gain its protein-degrading ability. | ||
The NAPase molecule provided shows two NAPase molecules that are mirror images, so here is just <scene name='Sandbox_11/Just_one/2'>one</scene>. NAPase, along with the rest of the trypsin family, has an active site that consists of the "catalytic triad." This <scene name='Sandbox_11/Catalytic_triad/2'>catalytic triad</scene> is made up of three amino acid residues (H57, D102, and S195) that play a major role in binding the substrate and catalyzing proteolysis. The distance between these residues on the protein chain, and the complexity of folding one might imagine is occurring, help to demonstrate the value of the Pro region. | The NAPase molecule provided shows two NAPase molecules that are mirror images, so here is just <scene name='Sandbox_11/Just_one/2'>one</scene>. NAPase, along with the rest of the trypsin family, has an active site that consists of the "catalytic triad." This <scene name='Sandbox_11/Catalytic_triad/2'>catalytic triad</scene> is made up of three amino acid residues (H57, D102, and S195) that play a major role in binding the substrate and catalyzing proteolysis. The distance between these residues on the protein chain, and the complexity of folding one might imagine is occurring, help to demonstrate the value of the Pro region. | ||