Sentence examples for bound to the side from inspiring English sources

Exact(6)

Breakage generates a free 5' hydroxyl group and enzyme bound to the 3' side of the break, presumably via the 3' phosphate group.

With the wing-forward bound to the side of the scrum, the opposing half-back would then have to manoeuvre past them to tackle the player with the ball; this would increase the amount of time the half-back would have in possession of the ball before their opposite could tackle them.

The methionine portion of SAM is bound to the side chains of D76, recognizing the free α-amine, whereas R54 forms a bidentate interaction with the carboxylate group.

We observed multiple instances (n = 66) in which cortactin bound to the side of a filament where a daughter filament was later nucleated.

While we already measured the dissociation rates of the diVCA constructs from Arp2/3 complex when the latter is not bound to the side of a mother filament, the rates of dissociation from the filament-bound Arp2/3 complex (the nascent branch) might be different.

In this work, VirB4 is observed bound to the side of the CC, and the FLCC VirB4 interaction is not disrupted in versions of the CC where TraF/VirB10 has been progressively truncated from the N-terminal end (Wallden et al, 2012).

Similar(54)

From the LigPlus result (Fig. 3), we could easily find that Zn2+ was bound to the side-chains of HIS186, HIS190, HIS196, TYR 226 and a water molecule.

Meanwhile, the water molecule was also bound to the side-chain of Glu187 and TYR226, which was thought to be important in activating the water molecule during catalysis.

The 2-OG binding is less well conserved, and the cofactor coordinates the iron in a bidentate manner via its 2-oxo group and one of its 1-carboxylate oxygens, whereas the 5-carboxylate is usually bound to the side-chain of a basic residue (Arg/Lys) and to a hydroxyl group from a Ser/Thr or Tyr residue.

(C ) Lifetime plots of single cortactin molecules bound to the sides of polymerizing actin filaments, with data collected at two different laser intensities (measured at laser head).

In this complex, two β-Nrx LNS6 domains independently bind to the side of the NL dimer using their "hyper-variable surface" located at the bottom of the β-sandwich fold, which results in a unique 2∶2 stoichiometry.

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