Sandbox Reserved 954: Difference between revisions

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[[Image:Fonction2.jpg|600px]] [[Image:fonction1.jpg|900px]]

Prior to hydrolysis of the acyl-enzyme intermediate, the serpin rapidly undergoes the S-to-R transition. Since the <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> is still covalently attached to the protease via the ester bond, the S-to-R transition moves the protease from the top to the bottom of the serpin. http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0104935 At the same time, the protease is distorted into a conformation, where the acyl enzyme intermediate is hydrolysed extremely slowly. The protease thus remains covalently attached to the target protease and is thereby inhibited.

Prior to hydrolysis of the acyl-enzyme intermediate, the serpin rapidly undergoes the S-to-R transition. Since the <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> is still covalently attached to the protease via the ester bond, the S-to-R transition moves the protease from the top to the bottom of the serpin. http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0104935 At the same time, the protease is distorted into a conformation, where the acyl enzyme intermediate is hydrolysed extremely slowly. The the active site of the enzyme would be expected to break.The protease thus remains covalently attached to the target protease and is thereby inhibited.

[[Image:Gb-2006-7-5-216-1-l_-_Copie.jpg|600px]]

Sandbox Reserved 954: Difference between revisions

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@@ Line 55: / Line 55: @@
 [[Image:Fonction2.jpg|600px]] [[Image:fonction1.jpg|900px]]
-Prior to hydrolysis of the acyl-enzyme intermediate, the serpin rapidly undergoes the S-to-R transition. Since the <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> is still covalently attached to the protease via the ester bond, the S-to-R transition moves the protease from the top to the bottom of the serpin. http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0104935 At the same time, the protease is distorted into a conformation, where the acyl enzyme intermediate is hydrolysed extremely slowly. The protease thus remains covalently attached to the target protease and is thereby inhibited.
+Prior to hydrolysis of the acyl-enzyme intermediate, the serpin rapidly undergoes the S-to-R transition. Since the <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> is still covalently attached to the protease via the ester bond, the S-to-R transition moves the protease from the top to the bottom of the serpin. http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0104935 At the same time, the protease is distorted into a conformation, where the acyl enzyme intermediate is hydrolysed extremely slowly. The the active site of the enzyme would be expected to break.The protease thus remains covalently attached to the target protease and is thereby inhibited.
 [[Image:Gb-2006-7-5-216-1-l_-_Copie.jpg|600px]]