Sandbox Reserved 1709: Difference between revisions

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=== Anchor ===

The <scene name='90/904314/Anchor_domain/3'> anchor domain</scene> sticks out from the side of VKOR with the primary role of stabilizing the enzyme within the membrane. To accomplish this, hydrophilic ~~and hydrophobic~~ residues are ~~highly conserved with hydrophilic residues located~~ to interact with the outer hydrophilic leaflet of the bilipid membrane, while the hydrophobic residues on the anchor have strong interactions with the inner hydrophobic leaflet of the bilipid membrane. These ~~sufficient~~ interactions allow for VKOR to remain in the proper arrangement and proximity ~~within the membrane~~ for Vitamin K to ~~properly~~ bind to be activated to ~~achieve its biological~~ function.

The <scene name='90/904314/Anchor_domain/3'> anchor domain</scene> sticks out from the side of VKOR with the primary role of stabilizing the enzyme within the membrane. To accomplish this, hydrophilic residues are positioned to interact with the outer hydrophilic leaflet of the bilipid membrane, while the hydrophobic residues on the anchor have strong interactions with the inner hydrophobic leaflet of the bilipid membrane. These interactions allow for VKOR to remain in the proper membrane arrangement and proximity for Vitamin K to bind and be activated. These membrane interactions allow for VKOR to stabilize in the membrane for proper activation of Vitamin K and catalytic function of the enzyme.

== Function: Method of Coagulation ==

Sandbox Reserved 1709: Difference between revisions

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@@ Line 20: / Line 20: @@
 === Anchor ===
-The <scene name='90/904314/Anchor_domain/3'> anchor domain</scene> sticks out from the side of VKOR with the primary role of stabilizing the enzyme within the membrane. To accomplish this, hydrophilic and hydrophobic residues are highly conserved with hydrophilic residues located to interact with the outer hydrophilic leaflet of the bilipid membrane, while the hydrophobic residues on the anchor have strong interactions with the inner hydrophobic leaflet of the bilipid membrane. These sufficient interactions allow for VKOR to remain in the proper arrangement and proximity within the membrane for Vitamin K to properly bind to be activated to achieve its biological function.
+The <scene name='90/904314/Anchor_domain/3'> anchor domain</scene> sticks out from the side of VKOR with the primary role of stabilizing the enzyme within the membrane. To accomplish this, hydrophilic residues are positioned to interact with the outer hydrophilic leaflet of the bilipid membrane, while the hydrophobic residues on the anchor have strong interactions with the inner hydrophobic leaflet of the bilipid membrane. These interactions allow for VKOR to remain in the proper membrane arrangement and proximity for Vitamin K to bind and be activated. These membrane interactions allow for VKOR to stabilize in the membrane for proper activation of Vitamin K and catalytic function of the enzyme.
 == Function: Method of Coagulation ==