Sandbox 11: Difference between revisions

{{STRUCTURE_2oua |  PDB=2oua  |  SCENE=  }}   

''Nocardiopsis alba'' Protease A, or NAPase, is an acid-resistant homolog of <i>alpha</i>-lytic protease.  As such, NAPase and <i>alpha</i>-lytic protease are both kinetically stable proteases, meaning it is the large barrier to unfolding that keeps this protease in its 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 it comes with a price.  The barrier to folding is large, with <i>alpha</i>-lytic protease's half life for folding is 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.