Comparative analysis of thermophilic and mesophilic proteins using Protein Energy Networks.

ABSTRACT:

Background

Thermophilic proteins sustain themselves and function at higher temperatures. Despite their structural and functional similarities with their mesophilic homologues, they show enhanced stability. Various comparative studies at genomic, protein sequence and structure levels, and experimental works highlight the different factors and dominant interacting forces contributing to this increased stability.

Methods

In this comparative structure based study, we have used interaction energies between amino acids, to generate structure networks called as Protein Energy Networks (PENs). These PENs are used to compute network, sub-graph, and node specific parameters. These parameters are then compared between the thermophile-mesophile homologues.

Results

The results sho

SUBMITTER: Vijayabaskar MS 

PROVIDER: S-EPMC3009521 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature