What is it about?
Three-dimensional structure of the fluorescent protein WasCFP with a tryptophan-based chromophore has been determined by an X-ray method at pH 5.5, pH 8.0 and pH 10.0, with a resolution of 1.14, 1.25 and 1.5 Å, respectively. We showed that changes in the acidity of the media are accompanied by a synchronous change of the side chain conformations of the residues in the near-chromophore environment. Subsequent changes in the local H-bond network interacting with the chromophore lead to considerable alterations in the protein spectral properties as a consequence of reversible processes of ionization-protonation of the Trp chromophore. These experimental results have been supported by quantum chemistry calculations.
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Why is it important?
New approach for design of new fluorescent biomarkers based on the ionizable Trp based chromophore.
Perspectives
The article may focus the people attention to the new direction of gene engineering of biomarkers
Vladimir Pletnev
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This page is a summary of: Green/cyan WasCFP at pH 10.0, July 2016, Protein Data Bank, Rutgers University,
DOI: 10.2210/pdb5drg/pdb.
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