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Even though BbpThr582 and Leu584 could interact with the peptide by two pairs of main chain-main chain hydrogen bonds (Fig. 3C), the replacement to alanine might serve a similar role instead of breaking the interaction with the peptide according to the results here.
As this complex presumably forms under tension in vivo, Buckley et al. [ 74 ] investigated the effect of force by sequentially forming and breaking the interaction between E-cadherin:β-catenin:αEcatenin and an actin filament suspended between two optically trapped beads.
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The sensing mechanism of Pi was also investigated by scanning electron microscope (SEM) and X-ray diffraction (XRD), and the results indicated that the Pi ions inhibited the quenching effect via breaking the interactions between MOFs and ZnO QDs, and caused the collapsing of MOFs.
The enzyme can relieve this stress either by releasing the DNA to the downstream side, aborting transcript synthesis, and returning to the RPo, or by releasing the DNA to the upstream side, breaking the interactions of its trailing edge with the DNA, and escaping from the promoter.
Our results show that breaking the interactions that restrain the fusion peptide is rate-limiting both for virion arrest and for hemifusion at the pH of endosomes from which influenza virus penetrates (approximately 5 to 5.5); this interpretation is consistent with the dominance hierarchy of mutations that influence the threshold pH for fusion (Steinhauer et al., 1996).
This could in turn break the interaction between E35 and the hydrolytic water molecule.
Densitometric quantification revealed that the E581Q mutation can break the interaction by 50 ± 10percentt.
This can be resolved by additional buffer changes and repeated centrifugation to break the interaction with the vacuolar membrane, which can be collected at the bottom of the tube.
A quantitative measure of specificity of the interaction between the anti-CenH3 tip and its epitope in native complexes can be obtained by measuring the unbinding force exerted by the tip required to break the interaction between the anti-CenH3 antibody and its CenH3 target.
Our data show that RF3GTP binding induces large conformational changes in the ribosome, which break the interactions of the class I RF with both the decoding center and the GTPase-associated center of the ribosome, apparently leading to the release of the class I RF.
An artificially high recombination rate (Supplementary Fig. S21a and b) could also break the interactions.
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