Construction and characterization of a spectral probe mutant of troponin C: application to analyses of mutants with increased Ca2+ affinity.

@article{Pearlstone1992ConstructionAC,
  title={Construction and characterization of a spectral probe mutant of troponin C: application to analyses of mutants with increased Ca2+ affinity.},
  author={Joyce R. Pearlstone and Thor J. Borgford and Madhup Chandra and K Oikawa and Cyril M. Kay and Osnat Herzberg and John Moult and Anna Herklotz and Fernando C. Reinach and Lawrence B. Smillie},
  journal={Biochemistry},
  year={1992},
  volume={31 28},
  pages={
          6545-53
        }
}
A spectral probe mutant (F29W) of chicken skeletal muscle troponin C (TnC) has been prepared in which Phe-29 has been substituted by Trp. Residue 29 is at the COOH-terminal end of the A helix immediately adjacent to the Ca2+ binding loop of site I (residues 30-41) of the regulatory N domain. Since this protein is naturally devoid of Tyr and Trp, spectral features can be assigned unambiguously to the single Trp. The fluorescent quantum yield at 336 nm is increased almost 3-fold in going from the… CONTINUE READING

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