Here we explore the possibility of using light scattering technologies as an analytical tool for understanding structural features of a protein that might be responsible for initiating aggregative interactions. Using widely independent complementary experimental and computational techniques, we found that interaction parameters like Km in particular possess good correlation with residue specific descriptors for the model protein Bovine Serum Albumin. Such information can help rationally design protein engineering and/or formulation strategies for prolonged shelf-life of such products.
Keywords: Molecular dynamics; ProtDCal; Protein aggregation; Protein interaction parameters; Protein stability.
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