Sandbox 173: Difference between revisions
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===Visual Signal Transduction=== | ===Visual Signal Transduction=== | ||
<applet load='1u19' size='300' color='black' frame='true' align='right' caption='Residues Involved in Activation of Rhodopsin. The generated structure is from Chain A.'/> | <applet load='1u19' size='300' color='black' frame='true' align='right' caption='Residues Involved in Activation of Rhodopsin. The generated structure is from Chain A.'/> | ||
==== | ====Photoisomerization of 11-''cis'' Retinal==== | ||
The 11-''cis'' retinal (retinylidene) Schiff base functions as an [http://en.wikipedia.org/wiki/Inverse_agonist inverse agonist] and is prominently involved in the activation of rhodopsin. The primary step in rhodopsin photoactivation occurs in the | The 11-''cis'' retinal (retinylidene) Schiff base functions as an [http://en.wikipedia.org/wiki/Inverse_agonist inverse agonist] and is prominently involved in the activation of rhodopsin. The primary step in rhodopsin photoactivation occurs in the photoisomerization of rhodopsin, as light energy absorbed from a photon is converted into chemical energy. As a photon is absorbed by the retina, the 11-''cis'' retinylidene ligand is switched into an all-''trans'' retinal configuration<ref name="Article2"/>. In this extremely efficient <200 fs process, the protein-binding pocket, initially fitted to accommodate the 11-''cis'' conformation of the chromophore, is preserved, which restrains the relaxation of the chromophore. The strained relaxation of conformational energy changes the protein state into the active form<ref name="Article2"/>. | ||
====Adjustment and Thermal Relaxation of the Protein==== | ====Adjustment and Thermal Relaxation of the Protein==== | ||