We have applied the method of dynamic light scattering to analyse the lysozyme-ethanol interaction. For low ethanol concentration (below 4.3% (v/v)) no chemical denaturation process is observed. When the ethanol concentration grows above the triggering concentration the hydrodynamic radius of lysozyme increases, indicating the structural changes within the protein molecule. The observed structural modifications are attributed to dehydration and preliminary tertiary structure modification of the protein molecule.
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