Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli.

@article{Gopalan1997FluorescencePO,
  title={Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli.},
  author={Venkat Gopalan and Ralph Peter Golbik and Gideon Schreiber and A. R. Fersht and S. Altman},
  journal={Journal of molecular biology},
  year={1997},
  volume={267 4},
  pages={765-9}
}
Escherichia coli ribonuclease P (RNase P), a ribonucleoprotein complex which primarily functions in tRNA biosynthesis, is composed of a catalytic RNA subunit, M1 RNA, and a protein cofactor, C5 protein. The fluorescence emission spectrum of the single tryptophan residue-containing C5 protein exhibits maxima at 318 nm and 332 nm. Based on a comparison of the emission spectra of wild-type C5 protein and some of its mutant derivatives, we have determined that the 318 nm maximum could be the result… CONTINUE READING

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