Cargando…
Evolution of frustrated and stabilising contacts in reconstructed ancient proteins
Energetic properties of a protein are a major determinant of its evolutionary fitness. Using a reconstruction algorithm, dating the reconstructed proteins and calculating the interaction network between their amino acids through a coevolutionary approach, we studied how the interactions that stabili...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8260555/ https://www.ncbi.nlm.nih.gov/pubmed/33569610 http://dx.doi.org/10.1007/s00249-021-01500-0 |
_version_ | 1783718831531753472 |
---|---|
author | Crippa, Martina Andreghetti, Damiano Capelli, Riccardo Tiana, Guido |
author_facet | Crippa, Martina Andreghetti, Damiano Capelli, Riccardo Tiana, Guido |
author_sort | Crippa, Martina |
collection | PubMed |
description | Energetic properties of a protein are a major determinant of its evolutionary fitness. Using a reconstruction algorithm, dating the reconstructed proteins and calculating the interaction network between their amino acids through a coevolutionary approach, we studied how the interactions that stabilise 890 proteins, belonging to five families, evolved for billions of years. In particular, we focused our attention on the network of most strongly attractive contacts and on that of poorly optimised, frustrated contacts. Our results support the idea that the cluster of most attractive interactions extends its size along evolutionary time, but from the data, we cannot conclude that protein stability or that the degree of frustration tends always to decrease. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s00249-021-01500-0. |
format | Online Article Text |
id | pubmed-8260555 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-82605552021-07-20 Evolution of frustrated and stabilising contacts in reconstructed ancient proteins Crippa, Martina Andreghetti, Damiano Capelli, Riccardo Tiana, Guido Eur Biophys J Original Article Energetic properties of a protein are a major determinant of its evolutionary fitness. Using a reconstruction algorithm, dating the reconstructed proteins and calculating the interaction network between their amino acids through a coevolutionary approach, we studied how the interactions that stabilise 890 proteins, belonging to five families, evolved for billions of years. In particular, we focused our attention on the network of most strongly attractive contacts and on that of poorly optimised, frustrated contacts. Our results support the idea that the cluster of most attractive interactions extends its size along evolutionary time, but from the data, we cannot conclude that protein stability or that the degree of frustration tends always to decrease. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s00249-021-01500-0. Springer International Publishing 2021-02-11 2021 /pmc/articles/PMC8260555/ /pubmed/33569610 http://dx.doi.org/10.1007/s00249-021-01500-0 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Original Article Crippa, Martina Andreghetti, Damiano Capelli, Riccardo Tiana, Guido Evolution of frustrated and stabilising contacts in reconstructed ancient proteins |
title | Evolution of frustrated and stabilising contacts in reconstructed ancient proteins |
title_full | Evolution of frustrated and stabilising contacts in reconstructed ancient proteins |
title_fullStr | Evolution of frustrated and stabilising contacts in reconstructed ancient proteins |
title_full_unstemmed | Evolution of frustrated and stabilising contacts in reconstructed ancient proteins |
title_short | Evolution of frustrated and stabilising contacts in reconstructed ancient proteins |
title_sort | evolution of frustrated and stabilising contacts in reconstructed ancient proteins |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8260555/ https://www.ncbi.nlm.nih.gov/pubmed/33569610 http://dx.doi.org/10.1007/s00249-021-01500-0 |
work_keys_str_mv | AT crippamartina evolutionoffrustratedandstabilisingcontactsinreconstructedancientproteins AT andreghettidamiano evolutionoffrustratedandstabilisingcontactsinreconstructedancientproteins AT capelliriccardo evolutionoffrustratedandstabilisingcontactsinreconstructedancientproteins AT tianaguido evolutionoffrustratedandstabilisingcontactsinreconstructedancientproteins |