User:Lynmarie K Thompson/Sandbox 1
From Proteopedia
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caption='aspartate receptor ligand binding domain' /> | caption='aspartate receptor ligand binding domain' /> | ||
| - | This is the ligand binding domain of the aspartate receptor protein with aspartate bound. The | + | This is the ligand binding domain of the aspartate receptor protein with aspartate bound. The complete protein is much longer: it extends its alpha helices (from the bottom of the initial view) across the membrane into the cell and binds other proteins important for signaling. |
| - | <scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/2'> | + | <scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/2'>Restore initial view</scene> |
Revision as of 14:07, 14 April 2010
CBI Molecules
Molecules under study by members of the University of Massachusetts Amherst Chemistry-Biology Interface Program. Many of the molecules we study are featured at the Molecular Playground. Follow the links below to read nontechnical descriptions in Proteopedia.
Bacterial chemotaxis receptors, Thompson & Weis laboratories: Seena Koshy
Many bacteria can direct their swimming towards favorable environments. They detect molecules such as amino acids or sugars using receptors that bind these molecules and transmit a signal into the cell. This signal controls several proteins which ultimately control the motors that rotate the flagella to cause the cell to either continue swimming or to tumble. When an attractant molecule binds, it signals: "Things look good, keep swimming!" The opposite signal occurs when bacteria sense decreasing concentrations of attractant molecules: "Time to tumble and try a new swimming direction."
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This is the ligand binding domain of the aspartate receptor protein with aspartate bound. The complete protein is much longer: it extends its alpha helices (from the bottom of the initial view) across the membrane into the cell and binds other proteins important for signaling.
