title: GFP family: structural insights into spectral tuning.
abstract: Proteins homologous to green fluorescent protein (GFP) span most of the visible spectrum, offering indispensable tools for live cell imaging. Structural transformations, such as posttranslational autocatalytic and photo-induced modifications, chromophore isomerization, and rearrangements in its environment underlie the unique capacity of these proteins to tune their own optical characteristics. A better understanding of optical self-tuning mechanisms would assist in the engineering of more precisely adapted variants and in expanding the palette of GFP-like proteins to the near-infrared region. The latest advances in this field shed light upon multiple features of protein posttranslational chemistry, and establish some important basic principles about the interplay of structure and spectral properties in the GFP family.
authors: Chromoproteins Chemistry Research Group, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
authors: Alexey A
authors: AA
authors: Pakhomov
authors: Vladimir I
authors: VI
authors: Martynov
mesh_terms: D000818:Animals; D049452:Green Fluorescent Proteins / Q000737:chemistry* / Q000378:metabolism*; D008164:Luminescent Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D013050:Spectrometry, Fluorescence
chemical_list: D008164:Luminescent Proteins; C413663:fluorescent protein 583; D049452:Green Fluorescent Proteins