Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding.

@article{Dhar2010StructureFA,
  title={Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding.},
  author={Apratim Dhar and Antonios Samiotakis and Simon Ebbinghaus and Lea Nienhaus and Dirar Homouz and Martin Gruebele and Margaret S. Cheung},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 41},
  pages={
          17586-91
        }
}
We combine experiment and computer simulation to show how macromolecular crowding dramatically affects the structure, function, and folding landscape of phosphoglycerate kinase (PGK). Fluorescence labeling shows that compact states of yeast PGK are populated as the amount of crowding agents (Ficoll 70) increases. Coarse-grained molecular simulations reveal three compact ensembles: C (crystal structure), CC (collapsed crystal), and Sph (spherical compact). With an adjustment for viscosity… CONTINUE READING

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