Sandbox 719: Difference between revisions

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The DsRed fluorescent protein is a 28kDa polypeptide that emits a red color after an excitation because of the presents of a chromophore composed by 3 amino acids –Gln-Tyr-Gly- (residues 66-68)<ref>Fluorescent proteins from nonbioluminescent Anthozoa species. Matz MV, Fradkov AF, Labas YA, Savitsky AP, Zaraisky AG, Markelov ML, Lukyanov SA.. PubMed : [http://www.ncbi.nlm.nih.gov/pubmed/10504696 10504696]</ref>. The fold of our protein is very closed to the most common fluorescent protein, the Aequorea victoria Green Fluorescent Protein (avGFP). The primary sequence of those two proteins is 23% similar but in the immediate vicinity of the chromophore the primary structure is strictly conserved and theses several amino acid are probably essential for the chromophore formation. The DsRed protein is obligatory a tetramer in solution. The monomer is composed by 11-strand beta ~~barrel~~ with a coaxial helix.

The DsRed fluorescent protein is a 28kDa polypeptide that emits a red color after an excitation because of the presents of a chromophore composed by 3 amino acids –Gln-Tyr-Gly- (residues 66-68)<ref>Fluorescent proteins from nonbioluminescent Anthozoa species. Matz MV, Fradkov AF, Labas YA, Savitsky AP, Zaraisky AG, Markelov ML, Lukyanov SA.. PubMed : [http://www.ncbi.nlm.nih.gov/pubmed/10504696 10504696]</ref>. The fold of our protein is very closed to the most common fluorescent protein, the Aequorea victoria Green Fluorescent Protein (avGFP). The primary sequence of those two proteins is 23% similar but in the immediate vicinity of the chromophore the primary structure is strictly conserved and theses several amino acid are probably essential for the chromophore formation. The DsRed protein is obligatory a tetramer in solution. The monomer is composed by 11-strand <scene name='Sandbox_719/Sheet/1'>beta sheet</scene> with a coaxial <scene name='Sandbox_719/Helix/1'>helix</scene>.

==== The tetramer Interface ====

Sandbox 719: Difference between revisions

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 <Structure load='1G7K' size='370' frame='true' align='right' scene='Insert optional scene name here' />
-The DsRed fluorescent protein is a 28kDa polypeptide that emits a red color after an excitation because of the presents of a chromophore composed by 3 amino acids –Gln-Tyr-Gly- (residues 66-68)<ref>Fluorescent proteins from nonbioluminescent Anthozoa species. Matz MV, Fradkov AF, Labas YA, Savitsky AP, Zaraisky AG, Markelov ML, Lukyanov SA.. PubMed : [http://www.ncbi.nlm.nih.gov/pubmed/10504696 10504696]</ref>. The fold of our protein is very closed to the most common fluorescent protein, the Aequorea victoria Green Fluorescent Protein (avGFP). The primary sequence of those two proteins is 23% similar but in the immediate vicinity of the chromophore the primary structure is strictly conserved and theses several amino acid are probably essential for the chromophore formation.  The DsRed protein is obligatory a tetramer in solution.  The monomer is composed by 11-strand beta barrel with a coaxial helix.
+The DsRed fluorescent protein is a 28kDa polypeptide that emits a red color after an excitation because of the presents of a chromophore composed by 3 amino acids –Gln-Tyr-Gly- (residues 66-68)<ref>Fluorescent proteins from nonbioluminescent Anthozoa species. Matz MV, Fradkov AF, Labas YA, Savitsky AP, Zaraisky AG, Markelov ML, Lukyanov SA.. PubMed : [http://www.ncbi.nlm.nih.gov/pubmed/10504696 10504696]</ref>. The fold of our protein is very closed to the most common fluorescent protein, the Aequorea victoria Green Fluorescent Protein (avGFP). The primary sequence of those two proteins is 23% similar but in the immediate vicinity of the chromophore the primary structure is strictly conserved and theses several amino acid are probably essential for the chromophore formation.  The DsRed protein is obligatory a tetramer in solution.  The monomer is composed by 11-strand <scene name='Sandbox_719/Sheet/1'>beta sheet</scene> with a coaxial <scene name='Sandbox_719/Helix/1'>helix</scene>.
 ==== The tetramer Interface ====