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Exploring the Strength of Subunit Interfaces Using Guanidine Hydrochloride and Dynamic Light Scattering

Dynamic light scattering is used to determine changes in mass and mean diameter of particles. Through the combination of varying concentrations of guanidine hydrochloride with either monomeric or multimeric protein samples we have developed a novel approach using Dynamic Light Scattering that has allowed us to test not only the strength of a protein's subunit interface but also to test the stability of its tertiary structure. Model systems, such as monomeric Bovine Serum Albumin (BSA) and tetrameric hemoglobin, with a known dissociation pattern, are used as fundamental examples to this light scattering approach. Watermelon Glyoxasomal Malate Dehydrogenase (dimer), E. coli 3Phosphoglycerate Dehydrogenase (tetramer) and Bovine Glutamate Dehydrogenase (hexamer) are used as complex systems to further investigate the approach. By measuring DLS at different guanidine hydrochloride concentrations in the range 0–2M dissociation of the oligomers can be followed where little change in tertiary structure occurs. By including ligands in the guanidine hydrochloride solution this approach is shown to be sensitive enough to detect and quantitate ligand induced changes in the strength of subunit interactions.