Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules.

@article{Neumann2008BindingOT,
  title={Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules.},
  author={Liv Neumann and Francesco Spinozzi and Raffaele Sinibaldi and Franco Rustichelli and Markus P{\"o}tter and Alexander Steinb{\"u}chel},
  journal={Journal of bacteriology},
  year={2008},
  volume={190 8},
  pages={2911-9}
}
The surface of polyhydroxybutyrate (PHB) storage granules in bacteria is covered mainly by proteins referred to as phasins. The layer of phasins stabilizes the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. Phasin PhaP1(Reu) is the major surface protein of PHB granules in Ralstonia eutropha H16 and occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to… CONTINUE READING

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