Sentence examples for binding in the N-half from inspiring English sources

Previous studies on HKI demonstrate a cooperative effect of glucose binding in the N-half to subsequent binding in the C-half [42], [43].

This observation (i.e., that mutation of an inhibitory site would decrease enzyme activity) was unexpected and may have been caused by a structural change that adversely affected glucose binding in the N-half.

Furthermore, mutation of the N-terminal ATP binding site did not alter the catalytic activity of the enzyme, which suggests that either the mutated residue was not essential for N-terminal ATP binding, or ATP binding in the N-half of HKIII does not regulate the activity of the C-half.

Here, we demonstrate that mutation of the glucose- or G6P-binding sites in the N-half of HKIII impairs catalysis in the C-half.

This is in agreement with a study that identified one high-affinity binding site in the N-terminal half of RAP and one in the C-terminal half [ 13].

To eliminate potential binding sites in the N-terminal half of the cullin, we then used bacterially expressed GST-RBX1 in complex with the C-terminal fragment of CUL1 (amino acids 324-776) [ 33].

Furthermore, the C-terminal half of tRNase ZL retains all conserved motifs for proper catalytic function but has lost the flexible arm involved in substrate binding, whereas the N-terminal half has lost all active motifs but contains the flexible arm.

It is possible that a similar intramolecular interaction occurs in HKIII, and reduction in N-half glucose binding results in diminished C-half binding, and an overall reduction in activity; however, other possibilities cannot be excluded.

We further show that the isolated TPR domain of CHIP is sufficient for binding to the N-terminal half of LRRK2, but not to the C-terminal half of LRRK2 (Supplemental Figure S2).

However, there was no difference in the percent of N-half OPN (N-half OPN/OPN*100%) in T2DM patients with normal, mild and moderate renal insufficiency (P = 0.65).

While the pTyr-binding pocket, which is present in the N-terminal half and highly conserved in the SH2 domain, provides the basal affinity for ligand binding with approximately a half of the total binding free energy [ 62], the hydrophobic pocket present in the C-terminal half of an SH2 domain provides specificity towards a hydrophobic residue in a peptide ligand.