Fluorescence quenching in the DsbA prote
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Alain Sillen; Jens Hennecke; Daniela Roethlisberger; Rudi Glockshuber; Yves Enge
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Article
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1999
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John Wiley and Sons
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English
⚖ 253 KB
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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