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"url": "https://figshare.com/collections/Supplementary_material_from_De_novo_synthetic_biliprotein_design_assembly_and_excitation_energy_transfer_/4037237",
"additionalType": "Collection",
"name": "Supplementary material from \"De novo synthetic biliprotein design, assembly and excitation energy transfer\"",
"author": [
{
"name": "Joshua A. Mancini",
"givenName": "Joshua A.",
"familyName": "Mancini",
"@type": "Person"
},
{
"name": "Molly Sheehan",
"givenName": "Molly",
"familyName": "Sheehan",
"@type": "Person"
},
{
"name": "Goutham Kodali"
},
{
"name": "Brian Y. Chow",
"givenName": "Brian Y.",
"familyName": "Chow",
"@type": "Person"
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{
"name": "Donald A. Bryant",
"givenName": "Donald A.",
"familyName": "Bryant",
"@type": "Person"
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{
"name": "P. Leslie Dutton"
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{
"name": "Christopher C. Moser",
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"description": "Bilins are linear tetrapyrrole chromophores with a wide range of visible and near-visible light absorption and emission properties. These properties are tuned upon binding to natural proteins and exploited in photosynthetic light-harvesting and non-photosynthetic light-sensitive signalling. These pigmented proteins are now being manipulated to develop fluorescent experimental tools. To engineer the optical properties of bound bilins for specific applications more flexibly, we have used first principles of protein folding to design novel, stable and highly adaptable bilin-binding four-α-helix bundle protein frames, called maquettes, and explored the minimal requirements underlying covalent bilin ligation and conformational restriction responsible for the strong and variable absorbance, fluorescence and excitation energy transfer of these proteins. Biliverdin, phycocyanobilin and phycoerythrobilin bind covalently to maquette cysteines (Cys) in vitro. A blue-shifted tripyrrole (TPB) formed from maquette-bound PCB displays a quantum yield of 26%. Although unrelated in fold and sequence to natural phycobiliproteins, bilin lyases nevertheless interact with maquettes during co-expression in Escherichia coli to improve the efficiency of bilin binding and alter bilin conformation. Bilins bind in vitro and in vivo to Cys residues placed in loops, towards the amino end or in the middle of helices but bind poorly at the carboxyl end of helices. Bilin-binding efficiency and fluorescence yield are improved by Arg and Asp residues adjacent to the ligating Cys on the same helix and by His residues on adjacent helices.",
"license": "https://creativecommons.org/licenses/by/4.0",
"keywords": "Biophysics, 90301 Biomaterials, FOS: Medical engineering, 60104 Cell Metabolism, FOS: Biological sciences, 60199 Biochemistry and Cell Biology not elsewhere classified, 69999 Biological Sciences not elsewhere classified, 30402 Biomolecular Modelling and Design, FOS: Chemical sciences",
"dateCreated": "2018-03-21",
"datePublished": "2018",
"dateModified": "2018-03-21",
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}