## Abstract Clarifying the contribution of tryptophan (Trp) to electronβtransfer (ET) processes in different protein surroundings can help to understand the effective pathway of ET in proteins. Interactions between Trp residues and protein microsurroundings involve intermolecular Hβbonds, cation an
An investigation of the electronic environment of tryptophan in proteins: Reliability of fluorescence quenching experiments
β Scribed by Fernanda Ricchelli
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 611 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1011-1344
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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