| Literature DB >> 18851577 |
F Zhang1, M W A Skoda, R M J Jacobs, S Zorn, R A Martin, C M Martin, G F Clark, S Weggler, A Hildebrandt, O Kohlbacher, F Schreiber.
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.Mesh:
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Year: 2008 PMID: 18851577 DOI: 10.1103/PhysRevLett.101.148101
Source DB: PubMed Journal: Phys Rev Lett ISSN: 0031-9007 Impact factor: 9.161