Sandbox27: Difference between revisions

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==~~This is a placeholder~~==

'''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!

~~This~~ is a ~~placeholder text~~ to ~~help you get started~~ in

==Bacteriorhodopsin==

~~placing~~ a ~~Jmol applet on your page. At any time~~, ~~click~~

Bacteriorhodopsin is an integral membrane protein used by organisms of the archaea domain, specifically halobacteria. It converts light energy to chemical energy by functioning as a proton pump that creates a proton gradient across the cell membrane. Bacteriorhodopsin subunits typically aggregate into a repeating hexagonal lattice that can cover up to half of the surface area of the cell. Retinal, a ligand found within the protein, changes its conformation upon the absorption of light. This results in a conformational change in the protein, which facilitates the proton pump ([http://en.wikipedia.org/wiki/Bacteriorhodopsin]).

~~"Show Preview" at~~ the ~~bottom of this page to see how it goes~~.

~~Replace~~ the ~~PDB id~~ (~~use lowercase!~~) ~~after~~ the ~~STRUCTURE_ and after PDB= to load~~

==Structure==

~~and display another~~ structure.

The <scene name='Sandbox27/Alpha_helices/1'>alpha helices</scene> shown in pink represent some of the hydrophobic elements throughout the crystallized structure of bacteriorhodopsin. The <scene name='Sandbox27/Beta_sheets/2'>beta strands</scene>, another type of hydrophobic element in the protein, are shown in purple, while the <scene name='Sandbox27/Ligands/4'>ligands</scene> (specifically, alpha-d-glucose, retinal, and 2,10,23-trimethyl-tetracosane) embedded within the protein are displayed in yellow.

Image of the 2-chain bacteriorhodopsin crystal structure crystallized from bicelles in archaeon halobacterium salinarum found at [[1kme]].

{{~~STRUCTURE_bacteriorhodopsin~~ | PDB=~~bacteriorhodopsin~~ | SCENE= }}

Contributors: Meenal Datta

Sandbox27: Difference between revisions

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@@ Line 1: / Line 1: @@
-==This is a placeholder==
+'''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!
-This is a placeholder text to help you get started in
+==Bacteriorhodopsin==
-placing a Jmol applet on your page. At any time, click
+Bacteriorhodopsin is an integral membrane protein used by organisms of the archaea domain, specifically halobacteria.  It converts light energy to chemical energy by functioning as a proton pump that creates a proton gradient across the cell membrane.  Bacteriorhodopsin subunits typically aggregate into a repeating hexagonal lattice that can cover up to half of the surface area of the cell.  Retinal, a ligand found within the protein, changes its conformation upon the absorption of light.  This results in a conformational change in the protein, which facilitates the proton pump ([http://en.wikipedia.org/wiki/Bacteriorhodopsin]).
-"Show Preview" at the bottom of this page to see how it goes.
-Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
+==Structure==
-and display another structure.
+The <scene name='Sandbox27/Alpha_helices/1'>alpha helices</scene> shown in pink represent some of the hydrophobic elements throughout the crystallized structure of bacteriorhodopsin.  The <scene name='Sandbox27/Beta_sheets/2'>beta strands</scene>, another type of hydrophobic element in the protein, are shown in purple, while the <scene name='Sandbox27/Ligands/4'>ligands</scene> (specifically, alpha-d-glucose, retinal, and 2,10,23-trimethyl-tetracosane) embedded within the protein are displayed in yellow.
+Image of the 2-chain bacteriorhodopsin crystal structure crystallized from bicelles in archaeon halobacterium salinarum found at [[1kme]].
-{{STRUCTURE_bacteriorhodopsin |  PDB=bacteriorhodopsin  |  SCENE=  }}
+{{STRUCTURE_1kme |  PDB=1kme  |  SCENE=  }}
+Contributors:  Meenal Datta