a. VR of TaqVP in ribbon representation. The main chain is in gray, side chains of variable amino acids are in green (sphere is glycine), and nonvariable aromatic amino acids are in orange. b. Surface representation of TaqVP, with the VR facing the viewer. Variable hydrophobic amino acids (I, V, and Y) are green, variable hydrophilic amino acids (S, N, D, and R) blue, and variable glycine pale orange. c. Superposition of the VR of TaqVP (red) and Mtd-P1 (orange) in Cα representation. The spheres represent the position of variable amino acids in each protein. d. Superposition of the VR of TaqVP (red) and TvpA (blue) in Cα representation. e. Superposition of the VR of TaqVP (red) and AvpA (magenta) in Cα representation. f. Stabilization of th...
<p>(A) Schematic presentation of the TCR formats. From left to right; scTCR wt, scTCR s, dsTCR, ct-d...
<p>(A) and (B) show the orientation of the two bound SBP tags (grey and orange) in a streptavidin te...
<p>The ribbons with different colors represent the four parts constituting the preproinsulin molecul...
a. TaqVP in ribbon representation (α-helices gold, β-strands blue, loops grey, and VR purple). The a...
<p>Numbers above the boxes indicate the amino acids and delimitate the functional domains of TAV: do...
<p>Left. Closeup of the YtvA chromophore (in green) with the amino acids considered in this study re...
<p>The H-bonds are highlighted in red. The different colors indicate the different locations of the ...
<p>Comparative schematic diagram for conserved surface accessible region (blue), previously recorded...
<p><b>Panel (A)</b> Amino acid entropy rates plot, x-axis: amino acid position; y-axis: entropy. The...
<p>A) Domain organization of the IT4var60 PfEMP1 protein with underlined the construct used in this ...
<p>(<b>A</b>) Amino acid compositions of all the 143 viable VP heptapeptide mutants. (<b>B</b>) Vari...
<p>A – GSH2 wild-type: Ile471 (red), Cys472 (yellow), Ala485 (blue) and Thr486 (green); B – GSH2-IC/...
<p>(A) Homodimer of apo-TaTPI is shown in carton representation, where α-helix, β-strand, and loop a...
<p>VB1, VB2, VB3, VB4, VB5, VB6, and VB7 are coloured in green, yellow, dark purple, pink, orange, r...
<p><b>A:</b> Schematic depiction and <b>B:</b> predicted 3D structural models of wild-type ApoC1 (H1...
<p>(A) Schematic presentation of the TCR formats. From left to right; scTCR wt, scTCR s, dsTCR, ct-d...
<p>(A) and (B) show the orientation of the two bound SBP tags (grey and orange) in a streptavidin te...
<p>The ribbons with different colors represent the four parts constituting the preproinsulin molecul...
a. TaqVP in ribbon representation (α-helices gold, β-strands blue, loops grey, and VR purple). The a...
<p>Numbers above the boxes indicate the amino acids and delimitate the functional domains of TAV: do...
<p>Left. Closeup of the YtvA chromophore (in green) with the amino acids considered in this study re...
<p>The H-bonds are highlighted in red. The different colors indicate the different locations of the ...
<p>Comparative schematic diagram for conserved surface accessible region (blue), previously recorded...
<p><b>Panel (A)</b> Amino acid entropy rates plot, x-axis: amino acid position; y-axis: entropy. The...
<p>A) Domain organization of the IT4var60 PfEMP1 protein with underlined the construct used in this ...
<p>(<b>A</b>) Amino acid compositions of all the 143 viable VP heptapeptide mutants. (<b>B</b>) Vari...
<p>A – GSH2 wild-type: Ile471 (red), Cys472 (yellow), Ala485 (blue) and Thr486 (green); B – GSH2-IC/...
<p>(A) Homodimer of apo-TaTPI is shown in carton representation, where α-helix, β-strand, and loop a...
<p>VB1, VB2, VB3, VB4, VB5, VB6, and VB7 are coloured in green, yellow, dark purple, pink, orange, r...
<p><b>A:</b> Schematic depiction and <b>B:</b> predicted 3D structural models of wild-type ApoC1 (H1...
<p>(A) Schematic presentation of the TCR formats. From left to right; scTCR wt, scTCR s, dsTCR, ct-d...
<p>(A) and (B) show the orientation of the two bound SBP tags (grey and orange) in a streptavidin te...
<p>The ribbons with different colors represent the four parts constituting the preproinsulin molecul...