Appropriate protein storage conditions are of interest for industrial biotechnology and an integral part to design sustainable biotechnological processes [1]. The molecular mechanisms need to be identified, that throughout the protein lifetime trigger possible but unwanted inactivation [2]. We developed a protocol here fore and discuss it on two systems:The conformational stability of bovine serum albumin (BSA) in solutions of different concentrations of ammonium sulfate was monitored in respect to thermal stabilty by differential scanning calorimetry (DSC), change of secondary structure was analyzed by attenuated total reflectance Fourier-transformation-infrared spectroscopy (ATR-FTIR) and conformational changes upon different ionic strengths were imaged by small-angle X-ray scattering (SAXS). In the second example we discuss the evaluation of the optimal formulation for 8 monoclonal immunoglobulin (IgMs). These were differentiated by DSC and SAXS. Optimized formulations prevented aggregation and fragmentation from shear stress, freeze-thaw cycles, accelerated storage and real time storage at 4°C and −20°C and also preserved immuno reactivity for 12 months. Highest conformational stability was characterized by SAXS. In particular the molecular mechanism for both systems were analyzed and a consistent picture developed, that explain the cause for stabilization. SAXS data indicate decoration of specific domains for both proteins. Mean forces calculated point towards a compaction of the proteins and their stabilization.[1] Monika Mueller, Maybelle Q. T. Loh, Doris H. Y. Tee, Yuansheng Yang and Alois Jungbauer (2013) Liquid Formulations for Long-Term Storage of Monoclonal IgGs. Applied Biochemistry and Biotechnology 169(4):1431-1448.[2] Rupert Tscheliesssnig, Alois Jungbauer, Rene Ueberbacher and Herwig Peterlik (2013) Protein stability at high kosmotropic salt level.submitted to Journal of Chemical Physics B.