Sentence examples for closure of the substrate from inspiring English sources

Since dimerization of the fluorescent halves in BiFC is demonstrated by fluorescence, we hypothesize that this additional dimerization interface provided by both fluorescent halves of the fluorescent protein induces a steric change e.g. closure of the substrate binding site.

We found that macrotopography favors cell attachment, and that bone-like tissue growth and organization are promoted by a tight "closure angle" of the substrate geometry.

The mechanism of action involves a hinge-bending motion that leads to domain closure once the substrate has bound to the active site.

The LDM provides a benchmark for the catalytic properties of TIM for a case in which there is minimal enzyme activation by loop closure over the substrate phosphodianion.

On the side distant from the substrate 3-carbonyl group, closure of the enzyme's β8−α8 loop is proposed to guide DHQ into the proximity of the Schiff base-forming Lys170.

Furthermore, we solved the crystal structures of apo-MeTr, CH3-H4-folate-bound MeTr, and H4-folate-bound MeTr, revealing a substrate-induced closure of the CH3-H4 folate binding cavity of MeTr.

After [H]-IAA injection, oocytes were placed in ice-cold Barth's solution for 10 min to allow substrate diffusion and closure of the injection spot.

The fact that AfUGMF66A has 200-fold lower kcat/ KM (Table 1) suggests that Phe66 plays an important role in catalysis that is unrelated to flap closure and establishing the correct conformation of the UDP part of the substrate.

Substrate plasticity produces partial closure of the cohesive zone upon full unloading (jump-out), residual tensile stresses at the front of the crack tip, and irreversible downward bending of the elastic film.

Thus, it can be conjectured that once Na+ and substrate have bound, it is the closure of the thin gates that triggers the transition to the inward-facing conformation.

In O-acetylserine sulfhydrylase, the interaction of the substrate carboxylate with a substrate-binding loop, highly conserved from bacteria to plants, triggers the closure of the active site to favor catalysis through proper positioning of substrate-binding groups and exclusion of water molecules [ 47– 47].