Abstract
Macromolecular crowding can alter the structure and function of biological molecules. We used small angle scattering to measure the change in size of a protein complex induced by macromolecular crowding. Crowding of the homodimer, superoxide dismutase (SOD) was induced using polyethylene glycol - 400, triethylene glycol, methyl-α-glucoside and trimethylamine N-oxide. Parallel small angle neutron scattering (SANS) and small angle x-ray scattering (SAXS) allowed us to unambiguously attribute apparent changes in radius of gyration to changes in the structure of SOD. We find that SOD is highly compressible for changes in volume up to 9%. Resistance to deformation beyond 9% increased dramatically.
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