User:Maggie Stopa/Sandbox 1: Difference between revisions

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==Structural Overview==
==Structural Overview==
<scene name='87/877513/Original_scene/1'>LPL</scene> is assumed to only be active as a <scene name='87/877513/Lpl_dimer/4'>homodimer</scene>, however, previous studies have argued that the lipase can be active in its <scene name='87/877513/Original_scene/1'>monomeric form</scene>. (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6442593/) The N-terminal domain of lipoprotein lipase is known to consist of an alpha/beta hydrolase domain, which is composed of six alpha helices and ten beta-strands. This domain creates an <scene name='87/877513/Alpha-beta_hydrolase_domain_1/1'>alpha beta hydrolase fold</scene>.The C-terminal domain of lipoprotein lipase is composed of twelve beta strands which form a "<scene name='87/877514/Just_barrel_domain_1/2'>barrel domain</scene>".
<scene name='87/877513/Original_scene/1'>LPL</scene> is assumed to only be active as a <scene name='87/877513/Lpl_dimer/4'>homodimer</scene>, however, previous studies have argued that the lipase can be active in its <scene name='87/877513/Original_scene/1'>monomeric form</scene>. (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6442593/) The N-terminal domain of lipoprotein lipase is known to consist of an alpha/beta hydrolase domain, which is composed of six alpha helices and ten beta-strands. This domain creates an <scene name='87/877513/Alpha-beta_hydrolase_domain_1/3'>alpha beta hydrolase fold</scene>.The C-terminal domain of lipoprotein lipase is composed of twelve beta strands which form a "<scene name='87/877514/Just_barrel_domain_1/2'>barrel domain</scene>".


==Mechanism==
==Mechanism==