User:Madeleine Wilson/Sandbox 1: Difference between revisions
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The secondary structure is composed of 10% <scene name='81/811086/Helices/3'>helices</scene> and 37% <scene name='81/811086/Beta_sheets/3'>beta sheets</scene>. The helical composition includes 3 <scene name='81/811086/Alpha_helices/4'>alpha helices</scene>, with two residing in the SET domain and one in the C-terminal domain. The alpha helices in the SET domain are two turns while the C-terminal helix is by far the largest with 4 turns. There are also 2 <scene name='81/811086/3-10_helices/4'>3-10 helices</scene> in the SET domain which are each one turn. There are 21 total beta strands which reside in the N-terminal domain and the SET domain. The beta strands are primarily anti-parallel and multiple antiparallel strands are connected by <scene name='81/811086/Type_i_beta_turns/3'>Type I</scene> and <scene name='81/811086/Type_ii_beta_turns/2'>Type II</scene> beta turns. | The secondary structure is composed of 10% <scene name='81/811086/Helices/3'>helices</scene> and 37% <scene name='81/811086/Beta_sheets/3'>beta sheets</scene>. The helical composition includes 3 <scene name='81/811086/Alpha_helices/4'>alpha helices</scene>, with two residing in the SET domain and one in the C-terminal domain. The alpha helices in the SET domain are two turns while the C-terminal helix is by far the largest with 4 turns. There are also 2 <scene name='81/811086/3-10_helices/4'>3-10 helices</scene> in the SET domain which are each one turn. There are 21 total beta strands which reside in the N-terminal domain and the SET domain. The beta strands are primarily anti-parallel and multiple antiparallel strands are connected by <scene name='81/811086/Type_i_beta_turns/3'>Type I</scene> and <scene name='81/811086/Type_ii_beta_turns/2'>Type II</scene> beta turns. | ||
===The N-terminal Domain=== | |||
[[Image:Example.jpg]] | |||
The N-terminal domain has no notable function in regard to the activity of KMT; however, it has been related to stability of the enzyme and most likely prevents its degradation within the cell. The N-terminal domain is highly conserved across species, which supports of the claim of necessity for stability. A Clustal alignment of a portion of the region shows a variety of high level species with conservation. | |||
===The C-Terminal Domain=== | ===The C-Terminal Domain=== | ||
