10.1371/journal.pone.0067290.g001 Céline M. Bourdin Céline M. Bourdin Bénédicte Moignot Bénédicte Moignot Lingxin Wang Lingxin Wang Laurence Murillo Laurence Murillo Marjorie Juchaux Marjorie Juchaux Sophie Quinchard Sophie Quinchard Bruno Lapied Bruno Lapied Nathalie C. Guérineau Nathalie C. Guérineau Ke Dong Ke Dong Christian Legros Christian Legros Primary structure analysis of TEH1-like auxiliary subunits of <i>P. americana</i>. Public Library of Science 2013 Biochemistry proteins ion channels protein structure Biomacromolecule-ligand interactions Macromolecular assemblies biophysics genetics gene expression RNA processing Molecular cell biology neuroscience Cellular neuroscience Molecular neuroscience neurophysiology teh1-like auxiliary subunits 2013-08-15 02:48:42 Figure https://plos.figshare.com/articles/figure/_Primary_structure_analysis_of_TEH1_like_auxiliary_subunits_of_P_americana_/773629 <p>A. Clustal W alignment of PaTEH1A (GenBank accession number KC206367), PaTEH1B (accession number KC206368) and DmTEH1 (accession number NP_649959). Transmembrane segments (M1 and M2) are indicated with bold line above the sequences. Conserved N-glycosylation sites are indicated by closed inverted triangles (▾) and O-glycosylation sites of PaTEH1s subunits are indicated by asterisk (*) (<a href="http://www.cbs.dtu.dk" target="_blank">www.cbs.dtu.dk</a>). Gaps are indicated by dashes. The undecapeptide (VALLDCEEDRT) and the decapeptide (YVPLSVHDTR) at the C-terminal ends of PaTEH1 variants are boxed. B. Hydrophobicity profile and deduced topological organization of PaTEH1A and PaTEH1B. Hydrophobicity analysis was performed using the algorithm of Kyte and Doolittle (1982). The amino acid residue position is plotted along the x-axis and the calculated mean hydrophobicity is plotted along the y-axis. Regions above the line are hydrophobic. The two putative membrane-spanning segments are indicated as M1 and M2.</p>