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The Emitting State of Tryptophan in Proteins with Highly Blue‐Shifted Fluorescence
Author(s) -
Broos Jaap,
TveenJensen Karina,
de Waal Ellen,
Hesp Ben H.,
Jackson J. Baz,
Canters Gerard W.,
Callis Patrik R.
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200700839
Subject(s) - tryptophan , fluorescence , indole test , azurin , yield (engineering) , domain (mathematical analysis) , chemistry , fluorescent protein , photochemistry , materials science , green fluorescent protein , amino acid , stereochemistry , biochemistry , optics , physics , mathematics , gene , mathematical analysis , electron transfer , metallurgy
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 1 L b state of indole, and not the 1 L a state. Nevertheless, these proteins are found to emit from 1 L a , except for a mutant of domain 1 (dI.M97V), which features the most blue‐shifted protein emission ever reported.
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