[Roughness of the globular protein surface].

The area and volume of the approximating ellipsoids taken from low resolution X-ray data have been calculated for 65 globular proteins. It has been shown that the dependence of these values on the protein molecular mass (M) coincides with those for even isometric bodies. This indicates that the asymmetry of globular proteins does not grow with the increase of their sizes. At the same time the 0.73 slope of the log-log dependence of the accessible surface area (A(s)) on the protein molecular mass differing from the value of 0.67 for even isometric bodies was observed (Miller S. et al., J. Mol. Biol. 1987. V.196. P.641). This can be explained by peculiarities of the protein surface. The method of molecule shape recovery by spherical harmonics has shown that the domain organization of protein molecule cannot explain the observed difference. Therefore the more detailed analysis of protein surface structure would be necessary.