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Interaction of proteins in solution from small angle scattering a perturbative approach
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Interaction of proteins in solution
from small angle scattering: a perturbative approach
Francesco Spinozzi 1, Domenico Gazzillo2, Achille Giacometti2, Paolo Mariani1 and Flavio Carsughi3
1 Istituto di Scienze Fisiche, Universita? di Ancona, and
INFM Unita? di Ancona, Via Brecce Bianche, I-60131 Ancona, Italy
2Dipartimento di Chimica Fisica, Universita? di Venezia, and
INFM Unita? di Venezia, S.Marta 2137, I- 30123, Venezia, Italy
3Facolta? di Agraria, Universita? di Ancona, and
INFM Unita? di Ancona, Via Brecce Bianche, I-60131 Ancona, Italy
(February 6, 2008)
In this work, an improved methodology for studying in-
teractions of proteins in solution by small-angle scattering,
is presented. Unlike the most common approach, where the
protein-protein correlation functions gij(r) are approximated
by their zero-density limit (i.e. the Boltzmann factor), we pro-
pose a more accurate representation of gij(r) which takes into
account terms up to the first order in the density expansion
of the mean-force potential. This improvement is expected to
be particulary effective in the case of strong protein-protein
interactions at intermediate concentrations. The method is
applied to analyse small angle X-ray scattering data obtained
as a function of the ionic strength (from 7 to 507 mM) from
acidic solutions of β-Lactoglobuline at the fixed concentration
of 10 g L?1. The results are compared with those obtained
using the zero-density approximation and show a significant
improvement particularly in the more demanding case of low
ionic strength.
Running Title: Interaction of proteins by SAS
Keywords: long-range interactions, mean-force potential,
density expansion, pair correlation functions, structure fac-
tor, β-Lactoglobuline
I. INTRODUCTION
The study of protein-protein interactions in solution
and the determination of both the physical origin of long
range interaction
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