User:Alex Pennington/Sandbox 1: Difference between revisions

(2 intermediate revisions by the same user not shown)

Line 17:

The ion channel of the protein is a 20 membered alpha helix bundle. This channel also contributes to the receptor function in three critical aspects: it contains a gating mechanism, it contains a water pore to stabalize ions, and it has a selectivity filter for ion charge. As with most transmembrane alpha helix bundles, it is hydrophobic around the edges to effectively be supported within the membrane, and it is hydrophilic on the inner portion to transport charged ions.

~~== Function ==~~

== Physiology ==

=== Physiology ===

The receptor is a cylidrically-shaped protein. It is embedded in the cell wall of post synaptic nerves at the skeletal neuromuscular junction. The receptor acts as a chemically controlled sodium (Na) channel also known as a [[ligand gated channel]].

Line 68:

Line 66:

'''F'''riday '''F'''asciculations

~~== Structural highlights ==~~

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

~~</StructureSection>~~

== References ==

~~<ref/>~~ Cholinesterase Inhibitors: Including Insecticides and Chemical Warfare Nerve Agents, ''Agency for Toxiz Substances and Disease Regulation'' '''accessed 5/2/14''' ~~<ref/>~~

1. Cholinesterase Inhibitors: Including Insecticides and Chemical Warfare Nerve Agents, ''Agency for Toxiz Substances and Disease Regulation'' '''accessed 5/2/14'''

~~<ref/>~~ Pierre-Jean Corringer and Jean-Pierre Changeux (2008) Nicotinic acetylcholine receptors. Scholarpedia, 3(1):3468. ~~<ref/>~~

2. Pierre-Jean Corringer and Jean-Pierre Changeux (2008) Nicotinic acetylcholine receptors. Scholarpedia, 3(1):3468.

~~<ref/> PMC2713585 <ref/>~~

3. Adcock C, Smith GR, Sansom MS. The nicotinic acetylcholine receptor: from molecular model to single-channel conductance. Eur Biophys J. 2000;29:29–37.

@@ Line 17: / Line 17: @@
 The ion channel of the protein is a 20 membered alpha helix bundle. This channel also contributes to the receptor function in three critical aspects: it contains a gating mechanism, it contains a water pore to stabalize ions, and it has a selectivity filter for ion charge. As with most transmembrane alpha helix bundles, it is hydrophobic around the edges to effectively be supported within the membrane, and it is hydrophilic on the inner portion to transport charged ions.
-== Function ==
+== Physiology ==
-=== Physiology ===
 The receptor is a cylidrically-shaped protein. It is embedded in the cell wall of post synaptic nerves at the skeletal neuromuscular junction. The receptor acts as a chemically controlled sodium (Na) channel also known as a [[ligand gated channel]].
@@ Line 68: / Line 66: @@
 '''F'''riday         '''F'''asciculations
-== Structural highlights ==
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
-</StructureSection>
 == References ==
-<ref/> Cholinesterase Inhibitors: Including Insecticides and Chemical Warfare Nerve Agents, ''Agency for Toxiz Substances and Disease Regulation'' '''accessed 5/2/14''' <ref/>
+. Cholinesterase Inhibitors: Including Insecticides and Chemical Warfare Nerve Agents, ''Agency for Toxiz Substances and Disease Regulation'' '''accessed 5/2/14'''
-<ref/> Pierre-Jean Corringer and Jean-Pierre Changeux (2008) Nicotinic acetylcholine receptors. Scholarpedia, 3(1):3468. <ref/>
+. Pierre-Jean Corringer and Jean-Pierre Changeux (2008) Nicotinic acetylcholine receptors. Scholarpedia, 3(1):3468.
-<ref/> PMC2713585 <ref/>
+. Adcock C, Smith GR, Sansom MS. The nicotinic acetylcholine receptor: from molecular model to single-channel conductance. Eur Biophys J. 2000;29:29–37.