NMR studies of the MgATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzyme.

@article{Fry1985NMRSO,
  title={NMR studies of the MgATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzyme.},
  author={David C. Fry and S A Kuby and Albert S Mildvan},
  journal={Biochemistry},
  year={1985},
  volume={24 17},
  pages={4680-94}
}
Proton NMR was used to study the interaction of beta,gamma-bidentate Cr3+ATP and MgATP with rabbit muscle adenylate kinase, which has 194 amino acids, and with a synthetic peptide consisting of residues 1-45 of the enzyme, which has previously been shown to bind MgepsilonATP [Hamada, M., Palmieri, R. H., Russell, G. A., & Kuby, S. A. (1979) Arch. Biochem. Biophys. 195, 155-177]. The peptide is globular and binds Cr3+ATP competitively with MgATP with a dissociation constant, KD(Cr3+ATP) = 35… CONTINUE READING

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