Additional file 1: Table S1. of Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments

Details of peptide properties. (PDF 60 kb

Additional file 4: Figure S3. of Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments

CD spectra for a negative control peptide from the P. falciparum formin display no folding under membrane-mimicking conditions. The peptide sequence is KKIPAPPPFLLKKK. (TIF 25 kb

Additional file 2: Figure S1. of Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments

Helical wheel predictions of all peptides from this study. (PDF 1382 kb

Additional file 5: Table S2. of Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments

Results from CD spectrum deconvolution of all 290 samples, with two different algorithms. (PDF 66 kb

Additional file 2: of Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins

Figure S2. Comparison of centrality analyses between wt-P2 and P2-F57A mutants. A residue interaction network (top) was generated from the crystal structures of P2 (bottom), and central residues were mapped onto them. A. Central residues globally conserved between wt-P2 and different P2-F57A mutant structures. Residues are considered central if their Z score ≥ 2, and they are coloured in the network as a function of this Z score with a gradient from yellow (Z score = 2) to red (Z score ≥ 4). Z score values of the wt-P2 were chosen for these Figs. B. Central residues only identified in one or several F57A mutant structures and not in wt-P2. Yellow is indicative of Z score ≥ 2. (PDF 1416 kb

Additional file 1: of Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins

Figure S1. DCCM analyses on earlier MD trajectories from P2 mutants. A. P38G. B. I42N. C. T50P. D. I51T. The empty structures are on the left and the palmitate-bound on the right. (PNG 3329 kb