Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

@article{Jackson1993BindingAH,
  title={Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.},
  author={Graham S. Jackson and Rosemary A. Staniforth and D J Halsall and T. Atkinson and J. John Holbrook and A. R. Clarke and Steven G. Burston},
  journal={Biochemistry},
  year={1993},
  volume={32 10},
  pages={2554-63}
}
Cpn60 was labeled with pyrene maleimide in order to follow structural rearrangements in the protein triggered by the binding of nucleotides and cpn10. The conjugate binds ATP, AMP-PNP, and ADP(P(i)) with pyrene fluorescence enhancements of 60%, 60%, and 15%, respectively. In each case, binding is cooperative with half-saturation (K1/2) occurring at 10 microM, 290 microM, and 2500 microM and Hill constants (nH) of 4, 3, and 3, respectively. Inclusion of the co-protein, cpn10, tightens the… CONTINUE READING