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

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Fig 2

Nitrogen-HSQC NMR spectra and secondary structure analysis of the MBP α2-peptide.

(A) The 1H-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 F 1 and F 2, 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 (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.