Insights on protein thermal stability: a graph representation of molecular interactions.

ABSTRACT:

Motivation

Understanding the molecular mechanisms of thermal stability is a challenge in protein biology. Indeed, knowing the temperature at which proteins are stable has important theoretical implications, which are intimately linked with properties of the native fold, and a wide range of potential applications from drug design to the optimization of enzyme activity.

Results

Here, we present a novel graph-theoretical framework to assess thermal stability based on the structure without any a priori information. In this approach we describe proteins as energy-weighted graphs and compare them using ensembles of interaction networks. Investigating the position of specific interactions within the 3D native structure, we developed a parameter-free network descriptor that permits

SUBMITTER: Miotto M 

PROVIDER: S-EPMC6662296 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature