Sandbox 11: Difference between revisions

One of the major features of NAPase is that each protease has two domains, an N domain and a C domain.  In this <scene name='Sandbox_11/Ntocrotatingone/1'>N to C Rainbow</scene>, one can see the N domain (red, orange, yellow), so-called because it contains the N-terminal amino acid, is connected covalently through the protein to the C domain (green, blue, violet).  The horizontal axis of this scene is the main dividing line between the domains, with few chains crossing the barrier.  It is important to note here that research suggests the first step to unfolding is when the two domains split.<ref>PMID:20195497</ref> Just ask Professor Jaswal.

Kelch (2007)<ref>PMID:17382344</ref>, looks at the differences between NAPase and αLP to try to understand what causes NAPase to be more acid resistant than αLP.  It is found that they form a similar number of salt-bridges (7 in NAPase, 8 in αLP), but the salt bridges are in different places.  Two of these bridges are conserved between the two, so there are five salt bridges that could be considered as important for acid resistance in NAPase.  The important difference between the location of bridges is that αLP has three bridges that span the N and C domains, while NAPase has none that span the domains.  The distance between the residues of each individual salt bridge in NAPase is relatively small(avg. distance = 20 residues), when compared to the large distance between the residues in αLP (avg. distance = 78 residues).  <scene name='Sandbox_11/Two_salt_bridges/2'>This picture</scene> shows the charged residues of Glutamate and Arginine, with red representing a negative charge, and blue representing a positive charge.