Picosecond tryptophan fluorescence of thioredoxin: evidence for discrete species in slow exchange.

@article{Merola1989PicosecondTF,
  title={Picosecond tryptophan fluorescence of thioredoxin: evidence for discrete species in slow exchange.},
  author={F. Merola and R. Rigler and A. Holmgren and J. Brochon},
  journal={Biochemistry},
  year={1989},
  volume={28 8},
  pages={
          3383-98
        }
}
The steady-state tryptophan fluorescence and time-resolved tryptophan fluorescence of Escherichia coli thioredoxin, calf thymus thioredoxin, and yeast thioredoxin have been studied. In all proteins, the tryptophan residues undergo strong static and dynamic quenching, probably due to charge-transfer interactions with the nearby sulfur atoms of the active cysteines. The use of a high-resolution photon counting instrument, with a time response of 60 ps full width at half-maximum, allowed the… Expand
Dissection of complex protein dynamics in human thioredoxin
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