The Emitting State of Tryptophan in Proteins with Highly Blue-Shifted Fluorescence
✍ Scribed by Jaap Broos; Karina Tveen-Jensen; Ellen de Waal; Ben H. Hesp; J. Baz Jackson; Gerard W. Canters; Patrik R. Callis
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 215 KB
- Volume
- 119
- Category
- Article
- ISSN
- 0044-8249
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The disulfide oxidoreductase DsbA is a strong oxidant of protein thiols and is required for efficient disulfide bond formation in the bacterial periplasm. DsbA contains two tryptophans: W76 and W126. The fluorescence of W76 changes upon reduction of the disulfide bridge, as analyzed previously (Henn
19 F nuclear magnetic resonance ( 19 F NMR) of 5-fluorotryptophan (5F-Trp) and tryptophan (Trp) fluorescence both provide information about local environment and solvent exposure of Trp residues. To compare the information provided by these spectroscopies, the four Trp residues in recombinant solubl