12 research outputs found

    The 3D view of the final system conformations.

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    The interface residues between two proteins TLRs (orange cartoon) and vaccines (magenta cartoon) residues (orange and magenta sticks) are labeled. Hydrogen bonds and hydrophobic contacts are presented as green dashed line and arc with spokes radiating, respectively. A and B indicate TLR4-construct 1 and TLR3-construct 2 complexes, respectively.</p

    S1 Fig -

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    Prediction of the secondary structure of the construct 1 (A) and construct 2 (B) vaccines. The predicted results showed that among 686 amino acids in the construct 1, 268 (39.07%), 135 (19.68%), 66 (9.62%) and 217 (31.63%) amino acids are involved in α-helix, extended strand, beta turn, and random coil, respectively. Our predicted outputs revealed that among 607 amino acids in the construct 2, 205 (33.77%), 132 (21.75%), 63 (10.38%) and 207 (34.10%) amino acids are involved in α-helix, extended strand, beta turn, and random coil, respectively. (DOCX)</p

    S2 Fig -

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    Linear (A and C) and Discontinuous (B and D) B-cell epitopes of the construct 1 (A and B) and construct 2 (C and D) vaccines (colored spheres). (DOCX)</p
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