File Name : fig 1s.tif

Caption : fig. 1s aromatic region of 1d 1h and of 1h-1h tocsy nmr spectra for tlr4 32aa peptide system, 0.5 mm, t 298 at ph 10.5 in meod-h2o solution. the free peptide is blue-coloured and the ni(ii)-bound is red; 1:1 ligand to metal molar ratio. the cross-correlations between h1 and h2 protons of histidine residues are highlighted by stars in the 2d spectrum. 

File Name : fig 2s.tif

Caption : fig. 2s selection of aliphatic region in the 1h-1h tocsy nmr spectra for tlr4 32aa peptide, 0.5 mm, t 298 k at ph 10.5 in meod-h2o solution, in the absence (blue) and in the presence (red) of 1 equivalent of ni(ii); the shift of hα and hβ protons from the three histidines is indicated .

File Name : fig 3s a.tif

Caption : fig. 3sa 1d 1h nmr spectra superimposition of aromatic  region for tlr4 32aa peptide, 2,5 mm, t 298 at ph 10.5 in dmso-d2o solution with increasing amounts of ni(ii) ion, from 1:0 to 1:0.4 ligand to metal molar ratio. filled blue and dotted red arrows indicate the signals of the peptide in the free and bound status, respectively. green labels and dashed arrows are for signals which disappeared following nickel addition.

File Name : fig 3s b.tif

Caption : fig. 3sb  1d 1h nmr spectra superimposition of  aliphatic region for tlr4 32aa peptide, 2,5 mm, t 298 at ph 10.5 in dmso-d2o solution with increasing amounts of ni(ii) ion, from 1:0 to 1:0.4 ligand to metal molar ratio. filled blue and dotted red arrows indicate the signals of the peptide in the free and bound status, respectively. green labels and dashed arrows are for signals which disappeared following nickel addition.

File Name : fig 4s a.tif

Caption : fig. 4sa selection of aromatic region in the 1h-13c hsqc nmr spectrum for tlr4 32aa peptide, 2.5 mm, t 298 k at ph 10.5 in dmso-d2o solution in the absence (blue) and the in presence (red) of 0.4 equivalent of ni(ii). filled blue and dotted red arrows indicate the signals of the peptide in the free and in the bound status, respectively.

File Name : fig 4s b.tif

Caption : fig. 4sb  selection of aromatic aliphatic region in the 1h-13c hsqc nmr spectrum for tlr4 32aa peptide, 2.5 mm, t 298 k at ph 10.5 in dmso-d2o solution in the absence (blue) and the in presence (red) of 0.4 equivalent of ni(ii). filled blue and dotted red arrows indicate the signals of the peptide in the free and in the bound status, respectively.

File Name : fig 4s c.tif

Caption : fig. 4sc  selection of  aliphatic region in the 1h-13c hsqc nmr spectrum for tlr4 32aa peptide, 2.5 mm, t 298 k at ph 10.5 in dmso-d2o solution in the absence (blue) and the in presence (red) of 0.4 equivalent of ni(ii). filled blue and dotted red arrows indicate the signals of the peptide in the free and in the bound status, respectively.