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

doi:10.1103/PhysRevLett.101.148101

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

School of Biosciences

Research output: Contribution to journal › Article › peer-review

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 language	English
Article number	148101
Number of pages	4
Journal	Physical Review Letters
Volume	101
Issue number	14
DOIs	https://doi.org/10.1103/PhysRevLett.101.148101
Publication status	Published - 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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10.1103/PhysRevLett.101.148101

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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.",

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T1 - Reentrant condensation of proteins in solution induced by multivalent counterions

AU - Zhang, F.

AU - Skoda, M.W.A.

AU - Jacobs, R.M.J.

AU - Zorn, S.

AU - Martin, Richard

AU - Martin, C.M.

AU - Clark, G.F.

AU - Weggler, S.

AU - Hildebrandt, A.

AU - Kohlbacher, O.

AU - Schreiber, F.

PY - 2008/10/3

Y1 - 2008/10/3

N2 - 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.

AB - 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.

KW - Negatively charged globular proteins

KW - trivalent counterions

KW - reentrant condensation behavior

KW - short-ranged electrostatic interactions

KW - multivalent cations

KW - acidic residues

KW - Monte Carlo simulations

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Reentrant condensation of proteins in solution induced by multivalent counterions

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