Allophycocyanin
From Proteopedia
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<Structure load='1all' size='300' frame='true' align='right' caption='allophycocyanin' scene='Insert optional scene name here' /> | <Structure load='1all' size='300' frame='true' align='right' caption='allophycocyanin' scene='Insert optional scene name here' /> | ||
| - | Allophycocyanin is a primarily <scene name='Allophycocyanin/2ndary_structure/2'>alpha-helical</scene> protein. It contains <scene name='Allophycocyanin/Subunits/2'>two subunits</scene>, which each have one phycocyanobilin. Allophycocyanin has a complex quaternary structure. First, trimers of the dimers form in a circular fashion, then stack on top of each other to form an antenna-like structure called the phycobilisome. | + | Allophycocyanin is a primarily <scene name='Allophycocyanin/2ndary_structure/2'>alpha-helical</scene> protein. It contains <scene name='Allophycocyanin/Subunits/2'>two subunits</scene>, which each have one phycocyanobilin. Allophycocyanin has a complex quaternary structure. First, <scene name='Allophycocyanin/Quaternary_structure/1'>trimers of the dimers</scene> form in a circular fashion, then <scene name='Allophycocyanin/Quaternary_structure_stack/1'>stack</scene> on top of each other to form an antenna-like structure called the phycobilisome. |
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| + | Allophycocyanin holds the <scene name='Allophycocyanin/Pigment/1'>pigment</scene> in place through a number of intermolecular interactions. A<scene name='Allophycocyanin/Asn73/1'>sn72</scene> forms hydrogen bonds with an amine in the pigment, while <scene name='Allophycocyanin/Arg86/1'>arginine 86</scene> interacts with a carboxylic acid that is exposed to the solvent. A key <scene name='Allophycocyanin/Asp87/2'>aspartic acid</scene> also holds the molecular planar. These interactions stabilize the pigment in the protein and hold the pigment planar. When the protein is unfolded, the | ||
Interestingly, the λmax of the chromophore can be tuned depending upon the protein binding it. For allophycocyanin, the λmax is 650 nm; in another phycobiliprotein, phycocyanin, the λmax is 625 nm, even though it uses the same chromophore. Phycocyanobilin is a highly flexible, linear tetrapyrrole that is covalently attached to the protein by a thiol linkage to a cysteine in the protein. | Interestingly, the λmax of the chromophore can be tuned depending upon the protein binding it. For allophycocyanin, the λmax is 650 nm; in another phycobiliprotein, phycocyanin, the λmax is 625 nm, even though it uses the same chromophore. Phycocyanobilin is a highly flexible, linear tetrapyrrole that is covalently attached to the protein by a thiol linkage to a cysteine in the protein. | ||
Revision as of 15:40, 4 November 2011
Blue-green algae such as Spirulina maximize their light harvesting ability by using phycobiliproteins to absorb light over a broader spectrum. One of these proteins, allophycocyanin, can be seen on the right. It contains a chromophore called .
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Allophycocyanin is a primarily protein. It contains , which each have one phycocyanobilin. Allophycocyanin has a complex quaternary structure. First, form in a circular fashion, then on top of each other to form an antenna-like structure called the phycobilisome.
Allophycocyanin holds the in place through a number of intermolecular interactions. A forms hydrogen bonds with an amine in the pigment, while interacts with a carboxylic acid that is exposed to the solvent. A key also holds the molecular planar. These interactions stabilize the pigment in the protein and hold the pigment planar. When the protein is unfolded, the
Interestingly, the λmax of the chromophore can be tuned depending upon the protein binding it. For allophycocyanin, the λmax is 650 nm; in another phycobiliprotein, phycocyanin, the λmax is 625 nm, even though it uses the same chromophore. Phycocyanobilin is a highly flexible, linear tetrapyrrole that is covalently attached to the protein by a thiol linkage to a cysteine in the protein.
