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The molecular basis for this selectivity was a different dissociation rate of the drug to a particular enzymatic form along the reaction pathway.
To explore the molecular basis for this selectivity, we synthesized and tested novel C5/C6-derivatives designed from quantum-based modeling of the interactions revealed in the co-crystal structures of PP5C in complex with cantharidin.
Molecular basis for this selectivity was examined by comparison of peptide maps of 32P-8-azido-cAMP-labelled or autophosphorylated peptides.
The molecular basis for this selectivity is not well understood, in large part because relatively little is known about the structure and function of miRNA gene promoters.
One possible basis for this selectivity is blood vessel permeability.
One basis for this selectivity might be related to the status of TLR3 in malignant cells.
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The molecular basis for the selectivity of this regulatory mechanism has to be better addressed and explained.
Full elucidation of the molecular basis of this selectivity is therefore needed to provide a framework for the rational design of feasible anti-HCV drugs or intervening applications.
The molecular basis of this selectivity remains unknown.
To examine the structural basis of this selectivity, we compared the sequences and structures of these two proteins.
Using molecular modelling and biochemical studies, we explain the basis of this selectivity.
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