Sandbox 420: Difference between revisions
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<tr id=' Acidic Polar Amino Acids'><td class="sblockLbl"><b>[[Acidic Polar Amino Acids]]</b></td><td class="sblockDat"></td></tr> | <tr id=' Acidic Polar Amino Acids'><td class="sblockLbl"><b>[[Acidic Polar Amino Acids]]</b></td><td class="sblockDat"></td></tr> | ||
</table> | </table> | ||
[[Image:Cannabinoid_Receptor_1_Amino_Acid_Residues.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. | ||