<p><b>(A)</b> Original SB056-lin, and <b>(B)</b> sequence-optimized β-SB056-lin. Yellow circles indicate hydrophobic residues, blue ones positively charged amino acids, and cyan indicates the polar serine residue.</p
<p>The pictograms show the relative orientation of the side chains on the upper (red) and lower side...
One peptide with the highest antigenicity score (calculated by EpiQuest-B) is displayed for each of ...
Superposition of the rainbow-colored structure of St I (A) [5] and St II (B) [4], with the black-col...
<p>The branched lysine is colored in blue. For the scrambled peptide (Sc_B4010) each copy contains t...
<p>(A): Alignment of amino acid sequences of the candidate OBPs. (B): Alignment of amino acid sequen...
a<p>PDB IDs from where the ‘C<sup>α</sup>NN’ motif segment residues are taken, residue number of PDB...
<p>The amino acid residues are consecutively numbered starting from the N-terminal of the mature pep...
<p>By default the output presents the hydrophilic residues as circles, hydrophobic residues as diamo...
<p><b>Fig. 2.A.</b> Schematic representation of the LGp/78 kDa glycoprotein (shaded bottom bar), Gn ...
<p>HsLin peptides are shown as a thick blue line in the same orientation as rHsAFP1; other residues ...
<p>Hydrophobic amino acids are yellow, negatively charged amino acids are red and positively charged...
<p>(A) P28-19 peptides corresponding to the underlined predicted hydrophilic sequence were synthesiz...
1<p>D-amino acid substitution.</p>a<p>Small underlined residues represent D-amino acids.</p><p>Amino...
<p>The helical wheel projection was performed using online program of the HeliQuest: <a href="http:/...
<p>(A), (B) and (C): superposition of LCMV (pink) with PV (blue) structures, with the peptide in sti...
<p>The pictograms show the relative orientation of the side chains on the upper (red) and lower side...
One peptide with the highest antigenicity score (calculated by EpiQuest-B) is displayed for each of ...
Superposition of the rainbow-colored structure of St I (A) [5] and St II (B) [4], with the black-col...
<p>The branched lysine is colored in blue. For the scrambled peptide (Sc_B4010) each copy contains t...
<p>(A): Alignment of amino acid sequences of the candidate OBPs. (B): Alignment of amino acid sequen...
a<p>PDB IDs from where the ‘C<sup>α</sup>NN’ motif segment residues are taken, residue number of PDB...
<p>The amino acid residues are consecutively numbered starting from the N-terminal of the mature pep...
<p>By default the output presents the hydrophilic residues as circles, hydrophobic residues as diamo...
<p><b>Fig. 2.A.</b> Schematic representation of the LGp/78 kDa glycoprotein (shaded bottom bar), Gn ...
<p>HsLin peptides are shown as a thick blue line in the same orientation as rHsAFP1; other residues ...
<p>Hydrophobic amino acids are yellow, negatively charged amino acids are red and positively charged...
<p>(A) P28-19 peptides corresponding to the underlined predicted hydrophilic sequence were synthesiz...
1<p>D-amino acid substitution.</p>a<p>Small underlined residues represent D-amino acids.</p><p>Amino...
<p>The helical wheel projection was performed using online program of the HeliQuest: <a href="http:/...
<p>(A), (B) and (C): superposition of LCMV (pink) with PV (blue) structures, with the peptide in sti...
<p>The pictograms show the relative orientation of the side chains on the upper (red) and lower side...
One peptide with the highest antigenicity score (calculated by EpiQuest-B) is displayed for each of ...
Superposition of the rainbow-colored structure of St I (A) [5] and St II (B) [4], with the black-col...