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.
Evolution of frustrated and stabilising contacts in reconstructed ancient proteins / Crippa, M.; Andreghetti, D.; Capelli, R.; Tiana, G.. - In: EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS. - ISSN 0175-7571. - ELETTRONICO. - 50:5(2021), pp. 699-712. [10.1007/s00249-021-01500-0]
|Titolo:||Evolution of frustrated and stabilising contacts in reconstructed ancient proteins|
|Data di pubblicazione:||2021|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1007/s00249-021-01500-0|
|Appare nelle tipologie:||1.1 Articolo in rivista|
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