# Characterization of graphs for protein structure modeling and recognition of solubility

arXiv: https://arxiv.org/abs/1407.8033 · HTML: https://mlsanity.com/paper/1407.8033/

## Key facts

- Cited by 1 papers in the map (data through 14 Oct 2026).
- First posted on arXiv 30 Jul 2014.

## Built on by (most cited first, 1 of 1)

- [Transferring Chemical and Energetic Knowledge Between Molecular Systems with Machine Learning](https://mlsanity.com/paper/2205.03339/) (2022)

## Abstract (arXiv)

This paper deals with the relations among structural, topological, and chemical properties of the E.Coli proteome from the vantage point of the solubility/aggregation propensity of proteins. Each E.Coli protein is initially represented according to its known folded 3D shape. This step consists in representing the available E.Coli proteins in terms of graphs. We first analyze those graphs by considering pure topological characterizations, i.e., by analyzing the mass fractal dimension and the distribution underlying both shortest paths and vertex degrees. Results confirm the general architectural principles of proteins. Successively, we focus on the statistical properties of a representation of such graphs in terms of vectors composed of several numerical features, which we extracted from their structural representation. We found that protein size is the main discriminator for the solubility, while however there are other factors that help explaining the solubility degree. We finally analyze such data through a novel one-class classifier, with the aim of discriminating among very and poorly soluble proteins. Results are encouraging and consolidate the potential of pattern recognition techniques when employed to describe complex biological systems.