Ionization, partitioning, and dynamics of tryptophan octyl ester: implications for membrane-bound tryptophan residues.

@article{Chattopadhyay1997IonizationPA,
  title={Ionization, partitioning, and dynamics of tryptophan octyl ester: implications for membrane-bound tryptophan residues.},
  author={Amitabha Chattopadhyay and Soumi Mukherjee and Raju Rukmini and Satinder S. Rawat and Swetha Sudha},
  journal={Biophysical journal},
  year={1997},
  volume={73 2},
  pages={839-49}
}
The presence of tryptophan residues as intrinsic fluorophores in most proteins makes them an obvious choice for fluorescence spectroscopic analyses of such proteins. Membrane proteins have been reported to have a significantly higher tryptophan content than soluble proteins. The role of tryptophan residues in the structure and function of membrane proteins has attracted a lot of attention. Tryptophan residues in membrane proteins and peptides are believed to be distributed asymmetrically toward… CONTINUE READING
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