Au-delà de l’état natif : de la structure protéique à la fonction à travers les paysages énergétiques et les ensembles conformationnels
DOI :
https://doi.org/10.18192/osurj.v5i1.8045Résumé
Plutôt que de considérer le repliement des protéines comme la formation d’une structure native unique, la biophysique moderne décrit les protéines comme des ensembles statistiques de conformations interconvertissantes dont les populations sont déterminées par la thermodynamique, la cinétique et le paysage énergétique imposé par les interactions moléculaires. Dans ce cadre, le pliage n’est pas considéré comme un événement discret, mais comme un processus dynamique. Lorsqu’ils sont placés dans un contexte cellulaire, ces ensembles conformationnels dynamiques sont couplés à la fonction des protéines et sont directement influencés par l’environnement intracellulaire et les protéines interagissant. Le repliement et la fonction des protéines suivent toujours les lois biophysiques, bien que leurs significations varient, et peuvent être décrits à l’aide de modèles cinétiques d’interactions intra- et intermoléculaires. Cette revue explore les déterminants biophysiques, biochimiques et cellulaires du repliement des protéines, en soulignant spécifiquement que le comportement des protéines est une propriété de la dynamique d’ensemble et de l’environnement intracellulaire.
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