Conformational changes in amyloid-beta (12-28) alloforms studied using action-FRET, IMS and molecular dynamics simulations (vol 6, pg 5040, 2015)

Steven Daly (1) , Alexander Kulesza (1) , Frederic Poussigue (1) , Anne-Laure Simon (1) , Chang Min Choi (1) , Geoffrey Knight (1) , Fabien Chirot (2) , Luke Macaleese (1) , Rodolphe Antoine (1) , Philippe Dugourd (1)

1 ILM - Institut Lumière Matière [Villeurbanne]
2 ISA-ANABIO-MS - Analyse biomoléculaire par spectrométrie de masse - Biological Analysis by Mass Spectrometry

There has been a consistent error in the name of the PDB code which was provided in the paper. The code given was 1LFM, but should have read 2LFM. There are 3 instances of this in the manuscript and one in the ESI. (1) The inset of Fig. 2 and the gure caption should appear as: Fig. 2 Representative structures simulated at 292 K of the dominant conformational family of the different charge states of the wild (top) and F19P (bottom) alloforms of Ab 12-28. Here, the donor chromophore (grafted to the C-terminal residue) is shown in red, the acceptor chromophore in blue, and the peptide backbone in green. The inset on the top panel shows the NMR structure (pdb database file 2LFM) for the full amyloid beta protein, with the 12-28 region highlighted in green. The corresponding figure of the ensembles with the alternative chromophore grafting location is shown in Fig. S2.

Domains: Chemical Sciences; Physics [physics]; Engineering Sciences [physics]

Steven Daly, Alexander Kulesza, Frederic Poussigue, Anne-Laure Simon, Chang Min Choi, et al.. Conformational changes in amyloid-beta (12-28) alloforms studied using action-FRET, IMS and molecular dynamics simulations (vol 6, pg 5040, 2015). Chemical Science, 2016, 7, pp.1609-1610. ⟨10.1039/c5sc90069g⟩. ⟨hal-02303924⟩