Sentence examples for substantially weaker binding from inspiring English sources

To evaluate whether LoNA binds to NCL through these binding motifs, we performed pulldown of biotinylated RNA and found that LoNA sequences harboring mutations M1 or M1 + M2 exhibited substantially weaker binding affinity to NCL compared to WT LoNA, whereas LoNA harboring mutations M2 had similar binding affinity to WT (Fig. 3f).

Although library screens were performed against αvβ3 integrin, the knottin peptides exhibited high affinity binding to both αvβ3 and αvβ5 integrins, which are often co-expressed on tumors or the tumor vasculature [18], [19], and substantially weaker binding to the structurally-related α5β1 and/or αiibβ3 integrins.

Further experiments with α1−835 and α1076−1160 fragments show substantially weaker binding, limiting strong DNA binding sites to the (HhH 2 domain and the OB-domain for double- and single-stranded DNA binding, respectively.

Adsorption of a fourth, fifth, or sixth H (D) adatom around a metal surface atom is energetically unfavorable, with substantially weaker binding compared to that on other surface sites.

AcNgn3KO showed substantially weaker binding to DNA than Ngn3, indicating that lysines play a greater role in contributing to stable DNA association in the presence of egg extract when these residues could be modified (Fig. 6B).

Our results show that the weaker binding state is able to bind to TPP, but is unable to form a tertiary docking interaction that completes the binding process.

FE65 S610A was found to bind strongly to APPc, but the binding of FE65 S610D to APPc is substantially weaker, indicating that Ser is a critical aa of APP FE65 interaction.

They found that this variant is substantially compromised in its catalytic efficiency (ca. 850-fold) due to weaker binding of the substrate and decreased catalytic activity.

A diphosphorylated peptide incorporating Ser487 located just upstream of Ser491 bound with ∼2- to 3-fold higher affinity, whereas binding to a peptide phosphorylated only at Ser487 was substantially weaker.

However, the unsubstituted phenyl-β-glucoside showed substantially weaker activation than either salicin (ortho substitution with a hydroxymethyl group) or 4-NP-β-glucoside (Fig. 6), suggesting that a larger (substituted) R group is required for optimal ligand binding (affinity), receptor activation (efficacy), or both.

The result isn't just fewer miraculous inventions, but substantially weaker growth.