Sandbox 420: Difference between revisions
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Secondary: The secondary structure of CB1 is made up of of ten α-helices and one β-sheet. 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 β-sheet. 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> | <scene name='71/716602/Normal/1'>Initial Scene (Reset)</scene> | ||
