Sandbox 420: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Tala Curry

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 ==Structure==
-'''Primary:''' The cannabinoid receptor (CB1) has a total of 472 amino acids. Of the 472 amino acids, 52.75% are nonpolar, 26.91% are uncharged polar, and 20.34% are polar (12.08% basic and 8.26% acidic). The location of the amino acid residues can be viewed by by selecting the name of each amino acid in the table below.
+===Primary===
+The cannabinoid receptor (CB1) has a total of 472 amino acids. Of the 472 amino acids, 52.75% are nonpolar, 26.91% are uncharged polar, and 20.34% are polar (12.08% basic and 8.26% acidic). The location of the amino acid residues can be viewed by by selecting the name of each amino acid in the table below.
 <table><tr><td colspan='2'>
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 [[Image:Cannabinoid_Receptor_1_Amino_Acid_Residues1.png]]
-'''Secondary:''' The secondary structure of CB1 is made up of of ten <scene name='71/716602/Alpha_helices/1'>α-helices</scene> and one <scene name='71/716602/Beta_sheet/1'>β-sheet</scene>. Of the ten α-helices, eight are roughly identical in size and align parallel to one another to form a typical transmembrane-type domain. The remaining two α-helices are shorter in length, run perpendicular to the other eight, and are located at one end of the receptor. On the opposite end of the receptor, an antiparallel β-sheet is located in the middle of the transmembrane domain formed by the eight parallel helices. While the structure overall has a low composition of polar amino acids, a large portion are located within this β-sheet, hinting at the role it may play in the function of the receptor.
+===Secondary===
+The secondary structure of CB1 is made up of of ten <scene name='71/716602/Alpha_helices/1'>α-helices</scene> and one <scene name='71/716602/Beta_sheet/1'>β-sheet</scene>. Of the ten α-helices, eight are roughly identical in size and align parallel to one another to form a typical transmembrane-type domain. The remaining two α-helices are shorter in length, run perpendicular to the other eight, and are located at one end of the receptor. On the opposite end of the receptor, an antiparallel β-sheet is located in the middle of the transmembrane domain formed by the eight parallel helices. While the structure overall has a low composition of polar amino acids, a large portion are located within this β-sheet, hinting at the role it may play in the function of the receptor.
 <scene name='71/716602/Normal/1'>Initial Scene (Reset)</scene>
-'''Tertiary:''' A homology model for the tertiary structure of CB1 is shown in the upper righthand of the page with the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref><ref>PMID:21638687</ref>.
+===Tertiary===
+A homology model for the tertiary structure of CB1 is shown in the upper righthand of the page with the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref><ref>PMID:21638687</ref>.
 ==Mechanism==