Correction: The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein

CORRECTION Correction: The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein The PLOS ONE Staff Fig 2 is missing from the PDF version of this paper. The publisher apologizes for the error. Please see Fig 2 in the online version of the article or below. OPEN ACCESS Citation: The PLOS ONE Staff (2015) Correction: The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein. PLoS ONE 10(7): e0131653. doi:10.1371/journal. pone.0131653 Published: July 1, 2015 Copyright: © 2015 The PLOS ONE Staff. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. PLOS ONE | DOI:10.1371/journal.pone.0131653 July 1, 2015 1/3 Fig 2. Nitrogen-HSQC NMR spectra and secondary structure analysis of the MBP α2-peptide. (A) The 1 H-15N HSQC spectrum of uniformly 13C-15N-labelled α2-peptide (S72-S107) dissolved in 20 mM HEPES-NaOH, 100 mM NaCl, and 10% D2O at a concentration of 1.47 mM, and recorded at 295 K. A total of 29 of 31 expected backbone peaks were assigned (there are 5 prolyl residues). The HSQC spectrum was processed by applying a 90°-shifted squared-sine bell function, and zero-filled up to 256 and 2048 complex points along F1 and F2, respectively, prior to Fourier transformation using NMRPipe. (B) Prediction of secondary structure probabilities for each residue (populations per residue) in the α2-peptide in aqueous solution, using a method designed for disordered proteins [68]. The method differentiates between α-helix PLOS ONE | DOI:10.1371/journal.pone.0131653 July 1, 2015 2/3 (blue), β-sheet (red), PPII (green), and random coil (not shown). The probabilities were calculated using the Hα, HN, Cα, Cβ, C’, and N chemical shift assignments for the α2-peptide. (C) Prediction of secondary structure probabilities for each residue in the α2-peptide in the presence of DPC, using a method designed for disordered proteins [49,68]. The Hα, HN, Cα, Cβ, C’, and N chemical shift assignments deposited in BMRB 6100 were used to calculate the secondary structure probabilities. (D) Secondary structure assignment methods used on the α2-peptide in the presence of DPC (PDB ID 2LUG). The XTLSSTR [91], PROSS [92], and SEGNO [93] methods all take into consideration PPII conformations, and differentiate them from coil, α, and β structures. The PROSS and SEGNO results were calculated using the “Polyproline” server created by the DSIMB bioinformatics team. The XTLSSTR results were obtained via the 2struc server created by the Wallace Laboratory [109]. The assignment indicates that the proline-rich region has a PPII conformation. doi:10.1371/journal.pone.0131653.g001 Reference 1. Vassall KA, Bessonov K, De Avila M, Polverini E, Harauz G (2013) The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein. PLoS ONE 8(7): e68175. doi: 10.1371/journal.pone.0068175 PMID: 23861868 PLOS ONE | DOI:10.1371/journal.pone.0131653 July 1, 2015 3/3  (...truncated)