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One weakness of the manuscript is that there is no clear exposition on if and why the two binding modes may have physiological consequences.
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We next considered how these different binding modes may account for the various activity profiles of compounds toward ERα.
In interpreting many previous SH3 binding experiments, new ligand binding modes may now need to be considered in the experimental interpretation.
Otherwise, the readers may feel that the two binding modes may be of peculiar novelty that may be of no physiological consequences.
This deviation from the results obtained by photo physical properties (MLCT excitation at 424 nm) indicate that a novel binding mode may be involved between the complex and the cellular environment which has altered its fluorescent nature.
This complex binding mode may explain the lower than expected significance of SMAP hits for known H3P targets, as the template for the binding site used for the SMAP screen did not capture the six-molecule ring binding mode.
This analysis, however, yielded no significant results, suggesting that the tRF binding mode may be more consistent with animal miRNAs.
Our analyses also allow us to infer how different modes of syntaxin binding may have arisen for Vps33p.
The similarity between CFTR and protein L suggests that these IgG-binding molecules may have a similar mode of interaction.
The complexes in a Homopharma present similar binding modes and have the conserved interacting residues.
The results of DNA-binding mode may be contributive in designing new and promising antimicrobial peptides for food preservatives.
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