Sandbox Reserved 427: Difference between revisions
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The tertiary structure consists of mainly <scene name="48/483884/Alpha_helices/2">alpha helices</scene>, which can be seen in pink. The quaternary structure of the protein consists of <scene name='48/483884/Twosubunits/1'>two subunits</scene> forming a complex. The structure is about 58 kDA in size and made up of 458 amino acids. | The tertiary structure consists of mainly <scene name="48/483884/Alpha_helices/2">alpha helices</scene>, which can be seen in pink. The quaternary structure of the protein consists of <scene name='48/483884/Twosubunits/1'>two subunits</scene> forming a complex. The structure is about 58 kDA in size and made up of 458 amino acids. | ||
=====Alpha Helical Domains===== | =====Alpha Helical Domains===== | ||
The Vitamin D binding protein consists of three alpha helical domains which are homologous. Domain I containing 10 aloha helices, <scene name='48/483884/Domain_ii/3'>Domain II</scene> 9, and Domain III 4 being shorter than the other domains. | The Vitamin D binding protein consists of <scene name='48/483884/Three_domains/2'>three alpha helical domains</scene> which are homologous. <scene name='48/483884/Domain_i/2'>Domain I</scene> containing 10 aloha helices, <scene name='48/483884/Domain_ii/3'>Domain II</scene> 9, and <scene name='48/483884/Domain_iii/2'>Domain III</scene> 4 being shorter than the other domains. | ||
=====Vitamin D Binding Protein and Human Serum Albumin===== | =====Vitamin D Binding Protein and Human Serum Albumin===== | ||
The overall structure is closely related to that of the human serum albumin, to which it is homologous. The proteins are very similar yet the three dimensional structure differs somewhat to facilitate binding. Looking at <scene name='48/483884/Evolutionaryconserved/2'>how the structure has evolved</scene> it can be seen that the outer edges are more variable while the core has more conserved sections. | The overall structure is closely related to that of the human serum albumin, to which it is homologous. The proteins are very similar yet the three dimensional structure differs somewhat to facilitate binding. Looking at <scene name='48/483884/Evolutionaryconserved/2'>how the structure has evolved</scene> it can be seen that the outer edges are more variable while the core has more conserved sections. | ||
