title: Small-angle neutron scattering study of structure and interaction during salt-induced liquid-liquid phase transition in protein solutions.
abstract: The liquid-liquid phase transition (LLPT) in aqueous salt solutions of lysozyme protein has been studied by small-angle neutron scattering. Measurements have been carried out on fixed protein concentration with varying salt concentration approaching LLPT. The data are fitted considering protein interaction by the two Yukawa (2Y) potential which combines short-range attraction and long-range repulsion. We show that LLPT arises because of enhancement of non-DLVO (Derjaguin-Landau-Verwey-Overbeek) short-range attraction without any conformational structural change of the protein. The salt concentration required for LLPT as well as corresponding short-range attraction decreases significantly with increase in protein concentration.
authors.affiliation: Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai-400085, India.
authors.forename: A J
authors.initials: AJ
authors.lastname: Chinchalikar
authors.forename: V K
authors.initials: VK
authors.lastname: Aswal
authors.forename: J
authors.initials: J
authors.lastname: Kohlbrecher
authors.forename: A G
authors.initials: AG
authors.lastname: Wagh
mesh_terms: D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D033363:Neutron Diffraction / Q000379:methods*; D044367:Phase Transition; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012492:Salts / Q000737:chemistry*; D053838:Scattering, Small Angle; D012996:Solutions / Q000737:chemistry*
chemical_list: D011506:Proteins; D012492:Salts; D012996:Solutions