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- W2394146782 abstract "Tryptophan analogs were biosynthetically incorporated into the tryptophan sites of DsbA protein to investigate the spectroscopic characteristics, local environments of tryptophans. This technique by using tryptophan-analog labeling may be of potential application to studying structure-function relationships and protein-protein interactions. 5-hydroxytryptophan labeled DsbA protein presents a fluorescence excitation wavelength at 315 rim and an emission near 340 rim. The chemical shifts of Trp76 and Trp126 in 5-fluorotrytophan labeled DsbA were identified in F-19-NMR spectra, and change of the chemical shift of Trp76. p can reflect the conformational change of DsbA protein during redox reaction. The future work is to use specific fluorescence and F-19-NMR of labeled DsbA protein to study its redox properties and interaction with substrates." @default.
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- W2394146782 date "2002-01-01" @default.
- W2394146782 modified "2023-09-27" @default.
- W2394146782 title "Study of the structural environment of DsbA protein by labeling of tryptophan analogs" @default.
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