The structure of chromophore-grafted Amyloid-β 12-28 dimers in the gas-phase: FRET-experiments guided modelling

Abstract : We present theoretical modelling, ion mobility spectrometry and action-FRET experiments for chromophore-grafted amyloid-β12–28 dimers. A first-principles global minimum search based on replica-exchange molecular dynamics (REMD) leads to a compact structure with strong interstrand interactions. We use REMD with a distance restraint that implements an adaptive effective bias upon average FRET-efficiencies and thus guides the sampling by the action-FRET measurement. This procedure leads to a pair of weakly interacting peptides. Ion-mobility confirms that the weakly interacting structure and not the global minimum with strongly interacting peptides is populated in the experiment. The presence of a high energy barrier between the two structural families, as evidenced from the MD data, suggests that a kinetically trapped structure is observed in the experiment.
Type de document :
Article dans une revue
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2016, 18 (13), pp.9061-9069. 〈10.1039/c6cp00263c〉
Liste complète des métadonnées

Littérature citée [60 références]  Voir  Masquer  Télécharger

https://hal.archives-ouvertes.fr/hal-01344513
Contributeur : Philippe Dugourd <>
Soumis le : mardi 12 juillet 2016 - 09:58:54
Dernière modification le : jeudi 6 septembre 2018 - 15:18:04

Fichiers

The structure of chromophore-g...
Fichiers produits par l'(les) auteur(s)

Identifiants

Collections

Citation

Alexander Kulesza, Steven Daly, Chang Min Choi, Anne-Laure Simon, Fabien Chirot, et al.. The structure of chromophore-grafted Amyloid-β 12-28 dimers in the gas-phase: FRET-experiments guided modelling. Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2016, 18 (13), pp.9061-9069. 〈10.1039/c6cp00263c〉. 〈hal-01344513〉

Partager

Métriques

Consultations de la notice

124

Téléchargements de fichiers

196