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

TL;DR

ProtFract is an open-access server that quantifies fractal properties of proteins, revealing subtle structural differences within Ras superfamily proteins that are not detectable by sequence analysis alone.

Contribution

It introduces a novel computational tool for analyzing fractal dimensions of protein properties, enhancing the understanding of structural symmetry and stability in protein families.

Findings

RAN proteins are most structurally stable.

ARFs have maximum unused hydrophobicity.

RAB interiors are least electrostatically conducive.

Abstract

Motivation: Protein surface roughness is fractal in nature. Mass, hydrophobicity, polarizability distributions of protein interior are fractal too, as are the distributions of dipole moments, aromatic residues, and many other structural determinants. The open-access server ProtFract, presents a reliable way to obtain numerous fractal-dimension and correlation-dimension based results to quantify the symmetry of self-similarity in distributions of various properties of protein interior and exterior. Results: Fractal dimension based comparative analyses of various biophysical properties of Ras superfamily proteins were conducted. Though the extent of sequence and functional overlapping across Ras superfamily structures is extremely high, results obtained from ProtFract investigation are found to be sensitive to detect differences in the distribution of each of the properties. For example, it was found that the RAN proteins are structurally most stable amongst all Ras superfamily proteins, the ARFs possess maximum extent of unused hydrophobicity in their structures, RAB protein interiors have electrostatically least conducive environment, GEM/REM/RAD proteins possess exceptionally high symmetry in the structural organization of their active chiral centres, neither hydrophobicity nor columbic interactions play significant part in stabilizing the RAS proteins but aromatic interactions do, though cation-pi interactions are found to be more dominant in RAN than in RAS proteins. Ras superfamily proteins can best be classified with respect to their class-specific pi-pi and cation-pi interaction symmetries. Availability: ProtFract is freely available online at the URL: http://bioinfo.net.in/protfract/index.html