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imb12089-sup-0001-figureS1.tif49K

Figure S1. Blue shift and increase in the intensity of fluorescence were observed when N-phenyl-1-naphthylamine (1-NPN) was bound to AlinOBP13. 1-NPN was dissolved in methanol and added to 50 mM Tris buffer (pH 7.4) at 5 μM, and the protein AlinOBP13 was also at 5 μM. When excited at 337 nm, 1-NPN in the Tris buffer produces a fluorescence peak with its maximum 450 nm, but in the presence of AlinOBP13, the emission wavelength is shifted to 405 nm accompanied by a sixfold increase in the intensity.

imb12089-sup-0002-figureS2.tif245K

Figure S2. Binding curves and Scatchard plots (insert) of the fluorescence probe N-phenyl-1-naphthylamine (1-NPN) to AlinOBP13. The dissociation constant of the AlinOBP13/1-NPN complex was 8.99 ± 0.90 μM.

imb12089-sup-0003-figureS3.tif81K

Figure S3. Binding curves and Scatchard plots for N-phenyl-1-naphthylamine (1-NPN) to the recombinant AlinOBP13 at three pH values (5.0, 7.4 and 10.0).

imb12089-sup-0004-figureS4.tif213K

Figure S4. Effect of sodium ion concentrations (0, 30, and 60 mM) on the binding affinities of AlinOBP13 to β-caryophyllene and trans-β-farnesene at pH 7.4.

imb12089-sup-0005-figureS5.tif681K

Figure S5. Comparison of binding abilities (1/Ki) of two other insect OBPs with their ligands at pH 7.4 and 10.0. Binding activity of AlinOBP11 to nerolidol and binding activity of HarmPBP1 to Z11–16:ALD.

imb12089-sup-0007-tableS1.docx14K

Figure S6. Predicted three-dimensional mode of AlinOBP13. Helices, N-terminal (N), and C-terminal (C) were labelled, and disulphide bridges were labelled yellow. Some hydrophobic and hydrophilic residues predicted as putative binding sites were displayed with green sticks.

imb12089-sup-0006-figureS6.tif582K

Table S1. Primers used in quantitative reverse transcriptase PCR and recombinant AlinOBP13 prokaryotic expression.

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