title: Structure-guided wavelength tuning in far-red fluorescent proteins.
abstract: In recent years, protein engineers have succeeded in tuning the excitation spectra of natural fluorescent proteins from green wavelengths into orange and red wavelengths, resulting in the creation of a series of fluorescent proteins with emission in the far-red portions of the optical spectrum. These results have arisen from the synergistic combination of structural knowledge of fluorescent proteins, chemical intuition, and high-throughput screening methods. Here we review structural features found in autocatalytic far-red fluorescent proteins, and discuss how they add to our understanding of the biophysical mechanisms of wavelength tuning in biological chromophores.
authors.affiliation: Department of Chemistry, University of Hawaii at Manoa, Honolulu, HI, USA; University of Hawaii Cancer Center, Honolulu, HI, USA. Electronic address: hng@hawaii.edu.
authors.forename: Ho-Leung
authors.initials: HL
authors.lastname: Ng
authors.affiliation: Department of Neurobiology, Stanford University, Stanford, CA, USA; Department of Bioengineering, Stanford University, Stanford, CA, USA; Department of Pediatrics, Stanford University, Stanford, CA, USA. Electronic address: mzlin@stanford.edu.
authors.forename: Michael Z
authors.initials: MZ
authors.lastname: Lin
mesh_terms: D000818:Animals; D055162:Biocatalysis; D019143:Evolution, Molecular; D008164:Luminescent Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000097573:Red Fluorescent Protein
chemical_list: D008164:Luminescent Proteins; D000097573:Red Fluorescent Protein