Journal
BIOINFORMATICS
Volume 35, Issue 15, Pages 2569-2577Publisher
OXFORD UNIV PRESS
DOI: 10.1093/bioinformatics/bty1011
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Funding
- Epigenomics flagship project EPIGEN
- Spanish Ministry of Economy and Competitiveness [BFU2014 - 55054 - P, BFU2017 - 86970 - P]
- Fundacio La Marato de TV3 [PI043296]
- European Research Council [RIBOMYLOME_309545]
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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 to distinguish thermostable and mesostable proteins with an accuracy of 76% and area under the receiver operating characteristic curve of 78%. Availability and implementation Code is available upon request to edoardo.milanetti@uniroma1.it Supplementary information Supplementary data are available at Bioinformatics online.
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