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Issue 13, 2016
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The structure of chromophore-grafted amyloid-β12–28 dimers in the gas-phase: FRET-experiment guided modelling

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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.

Graphical abstract: The structure of chromophore-grafted amyloid-β12–28 dimers in the gas-phase: FRET-experiment guided modelling

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Supplementary files

Article information


Submitted
13 Jan 2016
Accepted
12 Feb 2016
First published
19 Feb 2016

Phys. Chem. Chem. Phys., 2016,18, 9061-9069
Article type
Paper

The structure of chromophore-grafted amyloid-β12–28 dimers in the gas-phase: FRET-experiment guided modelling

A. Kulesza, S. Daly, C. M. Choi, A. Simon, F. Chirot, L. MacAleese, R. Antoine and P. Dugourd, Phys. Chem. Chem. Phys., 2016, 18, 9061
DOI: 10.1039/C6CP00263C

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