pSGB1 cosmid clone was selected based on the multiple bands binding with KS probe.
The Rh3d, Pt4f, O1s, Sr3d, Ti2p, C1s and valence band binding energy regions were scanned for all materials.
While the candidate collagen receptor amino acid sequences are essentially the same between the d and e1-band binding sites, the specific conformations of the sites are not.
This point is emphasised for the common conformation d-band binding site, where the collagen monomers have much less contact with decorons LRR's 2 through 8 (the central section), than at the e1-band receptor site.
This is superficially similar to our demonstration of discrete banded binding to salivary gland chromosomes, however we found that most of the binding in Drosophila may be a consequence of transcription, a possibility not considered in that study.
There is little difference in the binding affinity of the d and e1 band binding sites, although the specific conformation and packing of the collagen monomers produce differences in the strength of the interaction.
non-disordered variation between e1 and d band binding sites (axial plane) is accounted for simply from the microfibrillar structure: The collagen monomers are not 'straight-rods" in the gap region.
These are completely unrestricted when decoron is docked to the collagen fibril surface in the models presented here for the d and e1-band binding sites (Figures 2 and 3), as is the N-terminal attachment site for the AGAG chain (Ser 4, marked in yellow in Figure 3e).
This decrease in the binding affinity of proteins to lignin at pH 6.0 is further demonstrated by the pNP activities, where pNPG, pNPC, and pNPX activity loss in the supernatant correlates with the bands binding to lignin (Fig. 6c).
Analysis of 'Cordiale' showed only single bands binding to the ω-5 antibody in the total protein (Fig. 2E, lane 3) and monomeric gliadin fractions (Fig. 2E, lane 1), with no binding to the reduced residual protein fraction (Fig. 2E, lane 2).
