Sentence examples for essential to bind from inspiring English sources

Exact(4)

As a successive encoding of chunks of biometric templates is essential to bind sufficiently long keys distinct parts of the commitment may suffer from low entropy and, thus, are easily decoded [188], i.e., an adaption of biometric templates (e.g., [195]) or an improved use of error correction (e.g., [48]) is necessary.

FGly is catalytically active and "attacks" the sulfate moiety of substrates; it is essential to bind the substrate and also to hydrolyze the sulfate ester bond (36, 37).

The crystal structure of the heterodimer between the PB1 domains of p67 phox and p40 phox domain demonstrated that Lys-355 and Lys-382 in human p67 phox are essential to bind the PB1 domain of p40 phox [ 32, 76].

The crystal structure of the heterodimer of the PB1 domains from p67 phox and p40 phox [ 32] demonstrated that Lys-355 and Lys-382 in human p67 phox are essential to bind to the PB1 domain of p40 phox, and mutation of Lys-355 of human p67 phox abolished binding to p40 phox [ 76].

Similar(54)

Moreover, the structural flexibility of the p21 LH domain is essential to efficiently bind Cdk-cyclins and to initiate cell-cycle arrest.

This means that association of Beclin1 with these anti-apoptotic proteins is inhibitory for autophagy and their dissociation is essential to allow Beclin1 to bind to PIK3C3 and to initiate autophagy.

The binding function of the Hc domain is essential for BoNTs to bind the neuronal cell membrane, therefore, removal of the Hc domain results in a product that retains the endopeptidase activity of the LC but is non-toxic.

We had reported that the 8-nitrogen atom present in the 3-aryltropanes is not essential for tropanes to bind to monoamine uptake systems.

Furthermore, although W187 is directly essential for Ud/72 NS1 to bind host CPSF30 (thereby contributing to efficient inhibition of cellular pre-mRNA post-transcriptional processing [33]), PR8 NS1 inherently lacks this function [2].

Using the site-directed mutagenesis analysis, we confirmed that Q189 at the peroxidase site of COX II is essential for bioflavonoids to bind and re-activate its catalytic activity.

Further mapping experiments showed that the C-terminal less-conserved 10 residues of ABD-C are not essential for Nav1.2 to bind to ANK repeats.

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