Sandbox 173: Difference between revisions
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<applet load='1u19' size='300' color='black' frame='true' align='right' caption='Residues Involved in Activation of Rhodopsin. The generated structures are from Chain A.'/> | <applet load='1u19' size='300' color='black' frame='true' align='right' caption='Residues Involved in Activation of Rhodopsin. The generated structures are from Chain A.'/> | ||
====Photoisomeration of 11-''cis'' Retinal==== | ====Photoisomeration of 11-''cis'' Retinal==== | ||
The 11-''cis'' retinal (retinylidene) Schiff base functions as an inverse agonist and is prominently involved in the activation of rhodopsin. The primary step in rhodopsin photoactivation occurs in the photoisomeration 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>Article 2</ref>. 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>Article 2</ref>. | The 11-''cis'' retinal (retinylidene) Schiff base functions as an inverse agonist and is prominently involved in the activation of rhodopsin. The primary step in rhodopsin photoactivation occurs in the photoisomeration 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>Article 2</ref>. 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>Article 2</ref>. | ||
====Adjustment and Thermal Relaxation of the Protein==== | ====Adjustment and Thermal Relaxation of the Protein==== | ||