Small angle neutron scattering intensity distributions taken from cytochrome C and lysozyme protein solutions show a rising intensity at a very small wave vector Q, which can be interpreted in terms of the presence of a weak long-range attraction between protein molecules. This interaction has a range several times that of the diameter of the protein molecule, much greater than the range of the screened electrostatic repulsion. We show evidence that this long-range attraction is closely related to the type of anion present and ion concentration in the solution.
Effective Long-Range Attraction between Protein Molecules in Solutions Studied by Small Angle Neutron Scattering / Y. LIU; E. FRATINI; P. BAGLIONI; W.-R. CHEN; S.-H. CHEN. - In: PHYSICAL REVIEW LETTERS. - ISSN 0031-9007. - STAMPA. - 95:(2005), pp. 118102-1-118102-4. [10.1103/PhysRevLett.95.118102]
Effective Long-Range Attraction between Protein Molecules in Solutions Studied by Small Angle Neutron Scattering
FRATINI, EMILIANO;BAGLIONI, PIERO;
2005
Abstract
Small angle neutron scattering intensity distributions taken from cytochrome C and lysozyme protein solutions show a rising intensity at a very small wave vector Q, which can be interpreted in terms of the presence of a weak long-range attraction between protein molecules. This interaction has a range several times that of the diameter of the protein molecule, much greater than the range of the screened electrostatic repulsion. We show evidence that this long-range attraction is closely related to the type of anion present and ion concentration in the solution.
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