The significance of noise in the evolution of negative and positive cooperativity in protein complexes

Mostafa Taheri, Kazem Nouri, Yazdan Asgari, Zahra Zabihinpour, Mehdi Sadeghi

Résultats de recherche: Contribution à un journalArticleRevue par des pairs

3 Citations (Scopus)

Résumé

Evolution, tends to build complex structures out of protein molecules which has advantages for protein function. Few reasons have been proposed to explain this event. Some protein multimers show cooperativity in which binding of a ligand to a chain affect on the binding of other ligands. But it has remained unclear why cooperativity arises in positive or negative forms and what is the advantage of each of these forms. Our analysis, using deterministic and stochastic approaches, shows that the average and the standard deviation of ligand binding capacity indeed differ between positive and negative cooperativity. Considering standard deviation as a measure of noise in the system, our results demonstrate that the transition from negative to positive cooperativity is accompanied by an increase in the level of noise in the system. This source of noise enables the system to adapt in a fluctuating environment and could be subject to selection during evolution.

langue originaleAnglais
Pages (de - à)177-192
Nombre de pages16
journalMatch
Volume81
Numéro de publication1
étatPublié - 1 janv. 2019
Modification externeOui

Contient cette citation