Reentrant condensation of proteins in solution induced by multivalent counterions

F. Zhang, M.W.A. Skoda, R.M.J. Jacobs, S. Zorn, Richard Martin, C.M. Martin, G.F. Clark, S. Weggler, A. Hildebrandt, O. Kohlbacher, F. Schreiber

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Abstract

Negatively charged globular proteins in solution undergo a condensation upon adding trivalent counterions between two critical concentrations C* and C**, C*<C**. This reentrant condensation behavior above C** is caused by short-ranged electrostatic interactions between multivalent cations and acidic residues, mechanistically different from the case of DNA. Small-angle x-ray scattering indicates a short-ranged attraction between counterion-bound proteins near C* and C**. Monte Carlo simulations (under these strong electrostatic coupling conditions) support an effective inversion of charge on surface side chains through binding of the multivalent counterions.
Original languageEnglish
Article number148101
Number of pages4
JournalPhysical Review Letters
Volume101
Issue number14
DOIs
Publication statusPublished - 3 Oct 2008

Keywords

  • Negatively charged globular proteins
  • trivalent counterions
  • reentrant condensation behavior
  • short-ranged electrostatic interactions
  • multivalent cations
  • acidic residues
  • Monte Carlo simulations

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    Zhang, F., Skoda, M. W. A., Jacobs, R. M. J., Zorn, S., Martin, R., Martin, C. M., Clark, G. F., Weggler, S., Hildebrandt, A., Kohlbacher, O., & Schreiber, F. (2008). Reentrant condensation of proteins in solution induced by multivalent counterions. Physical Review Letters, 101(14), [148101]. https://doi.org/10.1103/PhysRevLett.101.148101