Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families

Author:

Parra R Gonzalo1ORCID,Freiberger Maria I2,Poley-Gil Miriam1,Fernandez-Martin Miguel1,Radusky Leandro G3,Ruiz-Serra Victoria1,Wolynes Peter G4,Ferreiro Diego U2,Valencia Alfonso15

Affiliation:

1. Computational Biology Group, Life Sciences Department, Barcelona Supercomputing Center , Barcelona, Spain

2. Laboratorio de Fisiología de Proteínas, Departamento de Química Biológica - IQUIBICEN/CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires , Buenos Aires C1428EGA, Argentina

3. Manas.tech , 300 Lenora Street 1541, Seattle, WA 98121, USA

4. Center for Theoretical Biological Physics and Department of Chemistry, Rice University , Houston, TX 77005, USA

5. Catalan Institution for Research and Advanced Studies (ICREA) , Barcelona, Spain

Abstract

Abstract According to the Principle of Minimal Frustration, folded proteins can only have a minimal number of strong energetic conflicts in their native states. However, not all interactions are energetically optimized for folding but some remain in energetic conflict, i.e. they are highly frustrated. This remaining local energetic frustration has been shown to be statistically correlated with distinct functional aspects such as protein-protein interaction sites, allosterism and catalysis. Fuelled by the recent breakthroughs in efficient protein structure prediction that have made available good quality models for most proteins, we have developed a strategy to calculate local energetic frustration within large protein families and quantify its conservation over evolutionary time. Based on this evolutionary information we can identify how stability and functional constraints have appeared at the common ancestor of the family and have been maintained over the course of evolution. Here, we present FrustraEvo, a web server tool to calculate and quantify the conservation of local energetic frustration in protein families.

Funder

Instituto de Salud Carlos III

European Union NextGenerationEU/PRTR

Consejo de Investigaciones Cientificas y Tecnicas

CONICET

Universidad de Buenos Aires

Center for Theoretical Biological Physics

Rice University

Barcelona Supercomputing Center

Publisher

Oxford University Press (OUP)

Reference21 articles.

1. Spin glasses and the statistical mechanics of protein folding;Bryngelson;Proc. Natl. Acad. Sci. U.S.A.,1987

2. Frustration in biomolecules;Ferreiro;Proc. Natl. Acad. Sci. U.S.A.,2014

3. Proteins: molecules defined by their trade-off;Bigman;Curr. Opin. Struct. Biol.,2020

4. Localizing frustration in native proteins and protein assemblies;Ferreiro;Proc. Natl. Acad. Sci. U.S.A.,2007

5. Frustration, function and folding;Ferreiro;Curr. Opin. Struct. Biol.,2018

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