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Quenching of Tryptophan Fluorescence by the Active-Site Disulfide Bridge in the DsbA Protein from Escherichia coli †

✍ Scribed by Hennecke, Jens; Sillen, Alain; Huber-Wunderlich, Martina; Engelborghs, Yves; Glockshuber, Rudi


Book ID
125492286
Publisher
American Chemical Society
Year
1997
Tongue
English
Weight
405 KB
Volume
36
Category
Article
ISSN
0006-2960

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Fluorescence quenching in the DsbA prote
✍ Alain Sillen; Jens Hennecke; Daniela Roethlisberger; Rudi Glockshuber; Yves Enge 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 253 KB 👁 2 views

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