Literature DB >> 18851577

Reentrant condensation of proteins in solution induced by multivalent counterions.

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.

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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


  26 in total

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9.  Effect of Temperature on Re-entrant Condensation of Globular Protein in Presence of Tri-valent Ions.

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