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An analysis of these complexes revealed that most of the native binding conformations were highly exposed to the solvent.
Similar(59)
Finally, 100 possible binding conformations were generated by AutoDock run.
Moreover the sampled conformations are highly dependent on the sequences of the peptides.
Aβ binding to PrPC is highly conformation-dependent, and only Aβo will interact with PrPC, with no binding detected in the presence of fibrillary or monomeric Aβ peptide [ 5, 7- 9].
These binding sites are highly charged.
Furthermore, the hydrophobic contacts formed by compounds 9 and 15 with Tyr385 suggest binding modes that are highly correlated with the conformation of naproxen and indomethacin inside COX-2 active site.
This result suggests that the most potent inhibitor in this series, compound 15, has a binding mode that is highly correlated with the conformation of naproxen inside COX-2 active site.
In this conformation, SFKs are free to engage intermolecular binding partners and are highly susceptible to phosphorylating and dephosphorylating enzymes.
Although the overall conformations assumed by GBA under these conditions were highly similar, small but critical differences in two loops localized at the mouth of active site were induced both by pH changes and by IFG binding.
The substrate-binding pocket is highly constrained.
Finally, the O state features two water channels into the proton-binding site that are highly similar to those seen in the L conformation, that is, open to the cytoplasm, while access from the periplasmic space is also occluded.
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