https://www.selleckchem.com/pr....oducts/ly2801653-mer
We resolve and track the release of counterions on the dPGS along its binding pathway with the plasma protein Human Serum Albumin (HSA). We find that the release of MCs remains favorable for the complexation leading to a considerable amount of release entropy as the driving force for complexation. The release of DCs only occurs above a certain DC concentration with a comparably smaller number of released ions than MCs. Its contribution to the binding free energy is small indicating a subtle cancellation between the entropy
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