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>