Do you have a DLS instrument available, such as one of the ones from Wyatt? If so, the experiment is very simple. You just put a solution of your protein in the cuvette and make the measurement. It is important to know a few things about the buffer (refractive index and viscosity), which can be estimated from tables based on the composition. Also, the sample must be free of dust, which can be accomplished by microcentrifugation. The hydrodynamic radius of the protein and its molecular weight can be determined with this measurement. It will also show if the protein is aggregated.

Thank you very much for the answer.

cheers

Also adding to Mr. Adams, you can take time scale measurements of your sample in that same cuvette or can keep it for next day reading, in case your protein is showing any structural changes like aggregation. Take a blank reading of the solution alone, in which protein is present. Thanks

thank you Subash also