Structures and interactions among globular proteins BSA and lysozyme are explored by small angle neutron scattering (SANS) technique at pD approximate to 7.0 by varying ethanol concentration. Interaction behaviours are also obtained in presence of monovalent salt (NaCI). SANS analysis shows that for both lower and higher BSA concentrations and in presence of NaCI, combination of intermediate -range repulsion and weak longrange attraction is responsible for the effective interaction behaviours with the variation of ethanol concentration. For lysozyme, interaction nature is same as BSA in absence of NaCi but in presence of NaCI, fractal structure factor explains the interaction behaviours. (C) 2017 Elsevier B.V. All rights reserved.