Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy.

@article{Otosu2010MultipleCS,
  title={Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy.},
  author={Takuhiro Otosu and Etsuko Nishimoto and Shoji Yamashita},
  journal={Journal of biochemistry},
  year={2010},
  volume={147 2},
  pages={191-200}
}
Human serum albumin (HSA) plays important roles in transport of fatty acids and binding a variety of drugs and organic compounds in the circulatory system. This protein experiences several conformational transitions by the change of pH, and the resulting conformations were essential for completing the physiological roles in vivo. Steady-state and time-resolved fluorescence spectroscopy was applied to single tryptophan residue solely arranged in HSA to study subtle conformational change around… CONTINUE READING
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