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The complementarities of two techniques, dynamic light scattering (DLS) and static light scattering detector coupled with a size exclusion chromatography system (SEC-LS), are illustrated by studying a number of samples where a thermally denatured and aggregated protein sample were dosed at different levels into a non-denatured protein sample.

In this application note, intrinsic viscosity measurements were performed on the sRAGE protein to establish whether the detector was able to detect and characterize the conformational change induced by the presence of calcium. Light scattering molecular weight measurements were also performed. Data are also presented showing that the conformation of sRAGE changes in the presence and absence of calcium.

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