The effects of ligands on the conformation of phosphoglycerate kinase: fluorescence anisotropy decay and theoretical interpretation.

@article{Mouawad1990TheEO,
  title={The effects of ligands on the conformation of phosphoglycerate kinase: fluorescence anisotropy decay and theoretical interpretation.},
  author={Liliane Mouawad and Michel Desmadril and David P{\'e}rahia and Jeannine M. Yon and Jean Claude Brochon},
  journal={Biopolymers},
  year={1990},
  volume={30 13-14},
  pages={
          1151-60
        }
}
Horse muscle phosphoglycerate kinase (PGK) is a monomer folded into two widely distant domains. In the glycolytic pathway, this enzyme catalyzes the first reaction that produces ATP. It was suggested, by analogy with yeast hexokinase, that a hinge-bending motion may be induced by the binding of specific substrates to the protein. To analyze such a motion, or any structural changes induced by ligand binding, fluorescence anisotropy decay of tryptophan residues in free and liganded PGK was… CONTINUE READING