Generation of bright monomeric red fluorescent proteins <i>via</i> computational design of enhanced chromophore packing
Sandrine Legault, Derek P. Fraser-Halberg, Ralph McAnelly, Matthew G. Eason, Michael C. Thompson, Roberto A. Chica
Abstract
-hydroxybenzylidene moiety is sandwiched between the side chains of Leu63 and Ile197, a structural motif that has not previously been observed in RFPs, and confirms that aliphatic packing leads to chromophore rigidification. Our results demonstrate that computational protein design can be used to generate bright monomeric RFPs, which can serve as templates for the evolution of novel far-red fluorescent proteins.
Topics & Concepts
ChromophoreQuantum yieldFluorescenceYield (engineering)Fluorescent proteinMonomerQuantumChemistryPhotochemistryGreen fluorescent proteinMaterials sciencePolymerOpticsPhysicsOrganic chemistryBiochemistryQuantum mechanicsGeneMetallurgyAdvanced Fluorescence Microscopy TechniquesPhotosynthetic Processes and MechanismsProtein Structure and Dynamics