Before the maturation of the chromophore, a fluorescent protein, just like any other three-dimensional protein structure, has to fold into the correct tertiary structure to function. We proposed that the evolutionarily conserved hinge residues, believed to be located on or near the lids of the fluorescent protein, are involved in the folding mechanism and rotation of the β-sheets and lids into the correct geometry. Acting like door hinges, these residues are translationally immobilized but rotationally active. Interference of the hinge sites may lead to allosteric effects and disruption of the protein’s functional motions. In the study, significant sequential and spatial conservation was found in conserved lid residues across 28 wild-type fluorescent proteins. Furthermore, the high rotational freedom and dihedral mobility of the conserved lid residues confirmed their behavior as hinge residues in the folding process.
Li, Binsen, "Exploration of Hinge Residues among GFP-like Proteins" (2013). Biology Honors Papers. 14.
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