Reentrant condensation of proteins in solution induced by multivalent counterions

Zhang, Fan and Skoda, M.W.A. and Jacobs, R.M.J. and Zorn, S. and Martin, Richard A. and Martin, C.M. and Clark, G.F. and Weggler, S. and Hildebrandt, A. and Kohlbacher, O. and Schreiber, F. (2008) Reentrant condensation of proteins in solution induced by multivalent counterions. Physical Review Letters: Moving Physics Forward, 101 (14). ISSN 0031-9007. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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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.

Item Type: Article
Additional information: Article Number: 148101
Subjects: Q Science > QC Physics
Divisions: Faculties > Science Technology and Medical Studies > School of Physical Sciences
Depositing User: Louise Dorman
Date Deposited: 27 Aug 2009 14:23
Last Modified: 23 Jun 2014 12:49
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