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Sandbox 38
From Proteopedia
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| + | ==Secondary Structure== | ||
<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here' /> | <Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here' /> | ||
| - | The <scene name='Sandbox_38/Adenylate_kinase_chain_a/1'>secondary structure</scene> of adenylate kinase is really cool. There are two <scene name='Sandbox_38/Adenylate_kinase_2o_structure/1'>types of secondary structure</scene>; the alpha-helices are highlighted in light green and the beta-sheets are highlighted in dark green. The <scene name='Sandbox_38/Adenylate_kinase_2o_structure/2'>hydrogen bonds</scene> are shown in yellow. | + | The <scene name='Sandbox_38/Adenylate_kinase_chain_a/1'>secondary structure</scene> of adenylate kinase is really cool. There are two <scene name='Sandbox_38/Adenylate_kinase_2o_structure/1'>types of secondary structure</scene>; the alpha-helices are highlighted in light green and the beta-sheets are highlighted in dark green. The <scene name='Sandbox_38/Adenylate_kinase_2o_structure/2'>hydrogen bonds</scene> are shown in yellow. They may be parallel or anti-parallel. |
| + | |||
| + | ==Residues== | ||
| + | The protein consists of <scene name='Sandbox_38/Adenylate_kinase_2o_structure/4'>hydrophobic</scene> and <scene name='Sandbox_38/Adenylate_kinase_2o_structure/5'>hydrophilic</scene> residues, highlighted in gray and red, respectively. | ||
Revision as of 19:02, 10 October 2012
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
Secondary Structure
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The of adenylate kinase is really cool. There are two ; the alpha-helices are highlighted in light green and the beta-sheets are highlighted in dark green. The are shown in yellow. They may be parallel or anti-parallel.
Residues
The protein consists of and residues, highlighted in gray and red, respectively.
