Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy.

@article{Mach1994SimultaneousMO,
  title={Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy.},
  author={Henryk Mach and C. Russell Middaugh},
  journal={Analytical biochemistry},
  year={1994},
  volume={222 2},
  pages={323-31}
}
A method for deconvolution of the near-uv second-derivative spectra of proteins into their component tryptophan, tyrosine, and phenylalanine spectra is described. In this approach, the second-derivative spectra of tryptophan and tyrosine model compounds are numerically shifted to create a set of reference spectra corresponding to anticipated peak positions in protein environments of different polarity. The relative contributions of these individual standard spectra are varied until the best fit… CONTINUE READING

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