Sandbox27: Difference between revisions
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'''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks! | |||
==Bacteriorhodopsin== | ==Bacteriorhodopsin== | ||
''' | 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]). | ||
==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_1kme | PDB=1kme | SCENE= }} | |||
Contributors: Meenal Datta | |||
