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={A. Dhar and Antonios Samiotakis and S. Ebbinghaus and L. Nienhaus and D. Homouz and M. Gruebele and M. Cheung},
  journal={Proceedings of the National Academy of Sciences},
  year={2010},
  volume={107},
  pages={17586 - 17591}
}
  • A. Dhar, Antonios Samiotakis, +4 authors M. Cheung
  • Published 2010
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences
  • 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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