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Motivation: Protein surface roughness is fractal in nature. Mass,hydrophobicity, polarizability distributions of protein interior are fractaltoo, as are the distributions of dipole moments, aromatic residues, and manyother structural determinants. The open-access server ProtFract, presents areliable way to obtain numerous fractal-dimension and correlation-dimensionbased results to quantify the symmetry of self-similarity in distributions ofvarious properties of protein interior and exterior.  Results: Fractal dimension based comparative analyses of various biophysicalproperties of Ras superfamily proteins were conducted. Though the extent ofsequence and functional overlapping across Ras superfamily structures isextremely high, results obtained from ProtFract investigation are found to besensitive to detect differences in the distribution of each of the properties.For example, it was found that the RAN proteins are structurally most stableamongst all Ras superfamily proteins, the ARFs possess maximum extent of unusedhydrophobicity in their structures, RAB protein interiors haveelectrostatically least conducive environment, GEM/REM/RAD proteins possessexceptionally high symmetry in the structural organization of their activechiral centres, neither hydrophobicity nor columbic interactions playsignificant part in stabilizing the RAS proteins but aromatic interactions do,though cation-pi interactions are found to be more dominant in RAN than in RASproteins. Ras superfamily proteins can best be classified with respect to theirclass-specific pi-pi and cation-pi interaction symmetries.  Availability: ProtFract is freely available online at the URL:http://bioinfo.net.in/protfract/index.html

ProtFract: A server to calculate interior and exterior fractal properties of proteins: Case study with Ras superfamily proteins