Solubility and Charge Inversion of Complexes of DNA and Basic Proteins

Overview

Journal Phys Rev Lett

Publisher American Physical Society

Specialty Biophysics

Date 2006 Oct 10

PMID 17026207

Citations 9

Authors

Eric Raspaud

J Pelta

M de Frutos

F Livolant

Affiliations

Soon will be listed here.

Abstract

The basic proteins, protamines and histones H1, are known to condense DNA in vivo. We examine here their ability to condense and solubilize in vitro linear DNA [and a synthetic polyanion, Poly(Styrene-Sulfonate) or PSS] at low ionic concentrations by varying the charge concentration ratio. Phase separation is observed in a very narrow range of ratios for short DNA and PSS; on both sides of this range, polydisperse and charged complexes are formed. A charge inversion is detected. For long DNA chains however, a different behavior is observed: the complexes are not soluble in excess of proteins.

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