Ancient braided fluvial systems were affected by a lack of binding vegetation, under variable paleoclimatic conditions, and possibly characterized by unique fluvial styles during the Precambrian.
In the case of APS serum proteins, their binding to CL is critically determined by the conformation and chemistry of the acyl chains, as demonstrated here by the lack of binding to the hydrogenated CL analogue, which shows baseline levels comparable with those of DCL.
This hypothesis is strengthened by the lack of binding of the anti-YFP nanobody onto the GFP/FLuc cell line since FLuc acts as an intracellular luciferase and reacts with its substrate d-luciferin intracellularly [[20]].
Intactness of the fragile borrelial outer membrane was confirmed by demonstrating lack of binding of antibodies directed against the periplasmic flagellar protein FlaB (Fig. 3C middle panels).
Specificity of this antibody was demonstrated by its lack of binding to a control viral antigen, cystovirus RNA polymerase, P2, isolated by Gottlieb et al [14] and BSA (Figure 3A).
The role of this structure in PfI2-PfPP1c interaction was substantiated by the lack of binding of PfI2 deleted for the region containing the α-helix (PfI2 (1–94)).
A requirement for GalNAc as the subterminal residue in this disaccharide is indicated by the lack of binding to glycans containing Galβ1-3GlcNAc (glycans 131 134) or Galβ1-3Gal (glycan 130).
This could be caused by the lack of binding of aPC to EPCR, explaining its lack of effect on the NF-κB pathway, the inflammatory process, monocyte TF expression, and mortality.
The importance of the latter interaction was confirmed by the lack of binding between Cg-Slx1 and Slx4CCD2, in which the C-terminal helix of the CCD is absent.
The wheat germ agglutinin-enriched lysate from the muscle biopsy of Case 5 showed α-dystroglycan hypoglycosylation as suggested by the lack of binding affinity to the glycoepitope-specific antibodies IIH6 and VIA4-1.
