Synergistic effect of temperature, protein and salt concentration on structures and interactions among lysozyme proteins in solution has been studied using small angle neutron scattering technique. Scattering study shows that for a particular protein concentration, with increasing temperature, short-range attraction decreases but long-range repulsion becomes system specific. In absence of salt, lower value of attractive interaction is obtained, however, in presence of salt it becomes higher and decreases with increasing temperature. For specific condition, weak long range attraction and intermediate range repulsion exists. At higher temperature (90 degrees C), fractal structure develops and the corresponding fractal dimension depends upon the experimental conditions. (C) 2016 Elsevier B. V. All rights reserved.