Consequences of cAMP and catalytic-subunit binding on the flexibility of the A-kinase regulatory subunit.

@article{Li2000ConsequencesOC,
  title={Consequences of cAMP and catalytic-subunit binding on the flexibility of the A-kinase regulatory subunit.},
  author={Fei Li and Milind Gangal and John M. Jones and Jason Deich and Kian Lovett and Susan S. Taylor and David S. Johnson},
  journal={Biochemistry},
  year={2000},
  volume={39 50},
  pages={15626-32}
}
A combination of site-directed labeling and time-resolved fluorescence anisotropy was used to further elucidate the structure and underlying dynamic features of the type I regulatory (R(I)(alpha)) subunit of the cAMP-dependent protein kinase. Specifically, the consequences of cAMP and the catalytic (C)-subunit binding on the backbone flexibility around seven sites of cysteine substitution and fluorescein maleimide labeling (Thr(6)Cys, Leu(66)Cys, Ser(75)Cys, Ser(81)Cys, Ser(99)Cys, Ser(145)Cys… CONTINUE READING

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