Publication | Open Access
The Emitting State of Tryptophan in Proteins with Highly Blue‐Shifted Fluorescence
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Citations
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References
2007
Year
Aldo-keto ReductaseMolecular BiologyBlue-shifted Protein EmissionPhototropinSingle Molecule BiophysicsHighly Blue‐shifted FluorescenceStructure-function Enzyme KineticsProteomicsPhotophysical PropertyProtein ChemistryDomain 1BiochemistryBiophotonicsSingle-molecule DetectionEmitting StateNatural SciencesMolecular BiophysicsPhosphorescenceTryptophan Residues
Kind of blue: Tryptophan residues embedded in rigid and hydrophobic protein matrices, like azurin and domain 1 of a transhydrogenase (dI), yield blue-shifted emission spectra with vibrational fine structure. These features are typical for emission from the 1Lb state of indole, and not the 1La state. Nevertheless, these proteins are found to emit from 1La, except for a mutant of domain 1 (dI.M97V), which features the most blue-shifted protein emission ever reported. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2007/z700839_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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