Sentence examples for binding pocket does not from inspiring English sources

The lack of a shift in the fluorescence emission spectrum of the W980 peptide in the presence of AtCML8 or AtCML9 suggests either that these CML (CaM-like) proteins do not bind to the peptide or that the binding pocket does not position the tryptophan residue in a hydrophobic environment.

The high specificity of the binding pocket does not result in high affinity; the KD determined by isothermal calorimetry is 11 μM.

The crystal structure (2.8 Å resolution) of c-Src (T338G) with N6- benzyl) ADP bouN6- benzylhADPthe creation of a unique nucleotide boundng pocket doeshows althatthe phospho-acreationbinding site of the kinase.

In addition, the absence of dark adaptation in both proteins indicates that the binding pocket does not easily accommodate a 13- cis-retinal configuration as previously suggested for NpSRII based on measurement of the rate of 13- cis-retinal regeneration.

Exopeptidases cleave near protein termini, and because the binding pockets do not exist are unable to accept any amino acids in some positions.

As the active site residues that constitute the chemically distinct binding pockets do not share the same p Ka values, the almost superimposing pH profile curves shown in Figure 3 refute a model involving separate binding sites for the two DCS binding events.

This suggests that dox binding to one of the effector-binding pockets does not affect binding to the second one, which is in agreement with published data showing that the binding of two Tc molecules to a TetR dimer occurs without significant cooperativity [ 31].

However, drug binding to the pocket does not prevent RKIP association with its inhibitory target, Raf-1, nor affect RKIP phosphorylation by Protein Kinase C at a regulatory site.

These results indicate that locostatin binding to the RKIP ligand pocket does not perturb RKIP/Raf-1 association nor alter MAPK activity.

N159 is located close to the NAD+ binding pocket, but does not directly interact with the substrate (Figure S5).

In the TTR∶OE1 structure, the halogenated phenyl ring moves away from the inner binding pocket and does not make significant interactions with the Ser117 and Ser117'.