Sandbox 11: Difference between revisions

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	''Nocardiopsis alba'' Protease A, or NAPase, is an acid-resistant homolog of <i>alpha</i>-lytic protease. As such, NAPase and <i>a</i>lp 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.		''Nocardiopsis alba'' Protease A, or NAPase, is an acid-resistant homolog of <i>alpha</i>-lytic protease. As such, NAPase and <i>a</i>lp 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.

	NAPase ~~has~~ two		The NAPase molecule provided shows two NAPase molecules that are mirror images, so here is just <scene name='Sandbox_11/Just_one/1'>one</scene>.