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Interaction of proteins in solution from small angle scattering a perturbative approach.pdf

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Interaction of proteins in solution from small angle scattering a perturbative approach

a r X i v : c o n d - m a t / 0 2 0 1 3 7 0 v 2 [ c o n d - m a t .s t a t - m e c h ] 2 2 J a n 2 0 0 2 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