Sandbox 11: Difference between revisions

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Eran Hodis, Student

Revision as of 17:16, 23 June 2010 view source Student (talk \| contribs) students 33,698 edits No edit summary ← Older edit		Revision as of 17:16, 23 June 2010 view source Student (talk \| contribs) students 33,698 edits No edit summary Newer edit →
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	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.		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.

	Kelch<ref>PMID:17382344</ref>, looks at the differences between NAPase and <i>alpha</i>-lytic protease to try to understand what causes NAPase to be more acid resistant that <i>alpha</i>-lytic protease. It is found that they form a similar number of salt-bridges (7 in NAPase, 8 in <i>alpha</i>-lytic protease), 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 <i>alpha</i>-lytic protease has three bridges that span the N and C domains, while NAPase has none that span the domains. (It is important to note here that research suggests that the first step to unfolding is when the two domains split.<ref>PMID:20195497</ref> Just ask Professor Jaswal, or look at reference 2.) <<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.		Kelch<ref>PMID:17382344</ref>, looks at the differences between NAPase and <i>alpha</i>-lytic protease to try to understand what causes NAPase to be more acid resistant that <i>alpha</i>-lytic protease. It is found that they form a similar number of salt-bridges (7 in NAPase, 8 in <i>alpha</i>-lytic protease), 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 <i>alpha</i>-lytic protease has three bridges that span the N and C domains, while NAPase has none that span the domains. (It is important to note here that research suggests that the first step to unfolding is when the two domains split.<ref>PMID:20195497</ref> Just ask Professor Jaswal, or look at reference 2.) <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.