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<Structure load='1f88' size='350' frame='true' align='right' caption='Retinal is in red, and scotopsin is in blue' scene='Insert optional ' /> | <Structure load='1f88' size='350' frame='true' align='right' caption='Retinal is in red, and scotopsin is in blue' scene='Insert optional ' /> | ||
<scene name='77/777643/Retinal_and_scotopsin/1'>Retinal and Scotopsin</scene> | <scene name='77/777643/Retinal_and_scotopsin/1'>Retinal and Scotopsin</scene> | ||
| - | == | + | == Genreal Information == |
| - | + | == Structure and Function == | |
| - | = | + | = Retinal = |
| - | = | + | = Scotopsin = |
| - | == Structural highlights == | ||
| - | Retinal is produced in the retina from vitamin A, from dietary beta-carotene. When rhodopsin absorbs light, its retinal cofactor isomerizes from the 11-cis to the all-trans configuration. | ||
| - | Lysine 296: In rhodopsin, the aldehyde group of retinal is covalently linked to the amino group of a lysine residue on the protein in a protonated Schiff base (-NH+=CH-) when it ligands to a metal atom. | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 23:15, 25 February 2018
Contents |
Bovine Rhodopsin
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