Microscopic surface structure of a globular molecule of ovalbumin in aqueous buffer solutions

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Abstract
The surface roughness (graininess) of a globular molecule of ovalbumin in aqueous buffer solutions was investigated through data from small‐angle x‐ray scattering in the Porod region. The scattering intensity I changes according to I = K 1 q −4 or I = K 1 q −4 + K 2. Here q is the wave vector, and K 1 and K 2 are constants. This means that the surface of the globular molecule does not have a fractalstructure, but the electron density transition is relatively sharp at the interface. The specific inner surfaceO s of the native globular molecule is approximately 1.7 times that of a sphere with a smooth surface. The value of O s is almost independent of the ovalbumin concentration and pH values, but increases with heat denaturation of the system.