The binding experiments did not reveal any significant difference in the inhibitory activity of peptide 15K in comparison with the scrambled analog (Figure 5D).
To ensure the tetramer-binding experiments did not underestimate the number of T cells that cross-react with both peptide variants, we analyzed intracellular IFNγ production by splenocytes from vaccinated mice stimulated with either the F1A5 or the WMF peptides (Fig. 2c, d).
In addition, even if predicted binding is real, these experiments do not provide direct evidence about the downstream effects of the binding (Gao et al., 2004).
Nine of the thirty-six regidentifiedinied in ChIP-chip experiments do not contain a GlnR binding motif.
However, our experiments do not indicate that the similar target profiles of p63 and p73 are due exclusively to binding by heterotetrameric complexes.
We conclude therefore that the high-affinity binding observed for 14-SASL in the EPR experiments does not correspond to binding to either the annular or nonannular binding sites and must correspond to binding to a site too distant from the Trp residues in KcsA to result in any fluorescence quenching.
Punctate labeling is diminished in images of tissue near the tracks of probes perfused with aCSF, which also exhibit diffuse TH labeling: control experiments did not reveal nonspecific binding, which indicates that the diffuse labeling is specific binding.
Thus, similar to the counter-selection cycles, the negative selection experiments did not reduce RNA binding to Aβ40 fibrils.
ITC experiments did not detect Cyr61 binding to the SMTB 1 44 domain in solution, and competitive ELISA showed that monomeric VTNC reacts weakly if at all with Cyr61; however, modified monomeric VTNC displays higher reactivity, suggesting that cryptic epitopes for Cyr61 were exposed by heat treatment as reported for VTNC interaction with specific antibodies [14], [29].
Eliminating DNA in these co-IP experiments did not alter the binding interactions we observed between TAF7L and PPARγ or TBP (data now shown).
