Sentence examples for tail of the substrate from inspiring English sources

The 3' tail of the substrate was then extended with 5'-TTCTTGATCAA-3' such that a stronger P2 could be formed (Figure S5).

On the other hand, the alkyl tail of the substrate is very floppy and experiences extensive conformational changes during the MD simulation.

The hydrophobic tail of the substrate would then supposedly be stabilized by residues of the TM helices at the N- and C-termini of yGPAA170 247, predicted to be involved in GPI interaction [ 1].

Although this residue was not on the surface of the modelled active site, it was directly behind the residues that contribute to the active site surface near the tail of the substrate analogue (approximately 8.5 Å away).

The branched C5 tail of the substrate resides in a pocket surrounded principally by hydrophobic residues, including Ala63, Phe76, Met79, Phe83, Ile86, Met90, Ile146, and Ile156, (4, panel a).

Based on the general model of VCP function within UPS, the target substrate is ubiquitinated by E1-E2-E3 enzyme candade and VCP engages the polyubiquitin tail on the substrate protein through the above cofactors.

They were actually associated with long tails of the substrate peak (i.e., critical truncation rods along hhh) but not with film components, as shown in reciprocal lattice maps around 222 STO reflections.

For each of the three structures, a difference map showing the scissile and C-terminal tail regions of the substrate, as well as the side chain of His 64 and the contents of the anion-binding pocket, was calculated before these components had been added to the structure, but after the remainder of the structure had been refined.

The broad and low intensity peak around 51° (see the triangle) is attributed to a diffraction tail of the Si substrate.

As mentioned previously, the tail of the IP substrate is sequestered within a hydrophobic binding pocket (4, panel a).

This suggests that a long, lipophilic tail can enhance the potency of potential GGTase-II inhibitors, presumably through interaction with the enzyme site that holds the tail of the natural substrate geranylgeranyl diphosphate.