Finite size and inner structure controlled by electrostatic screening in globular complexes of proteins and polyelectrolyte
نویسندگان
چکیده
We present an extended structural study of globular complexes made by mixing a positively charge protein (lysozyme) and a negatively charged polyelectrolyte (PSS). We study the influence of all the parameters that may act on the structure of the complexes (charge densities and concentration of the species, partial hydrophobicity of the polyion chain, ionic strength). The structures on a scale range lying from 10Å to 1000Å are measured by SANS. Whatever the conditions, the same 15
منابع مشابه
Charge stoichiometry inside polyelectrolyte-protein complexes: a direct SANS measurement for the PSSNa-lysozyme system.
We study by small angle neutron scattering and UV titration how the ratio of negative to positive charges, [-]/[+](intro), acts on the structure of complexes formed by short negatively charged polyelectrolyte chains (PSS) and globular positively charged proteins (lysozyme). The range of [-]/[+](intro) lies between 0.65 and 3.33. In all ratios, dense primary complexes are formed with radii aroun...
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