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A free energy component analysis makes possible the decomposition of the free energy difference between the binding of the wild-type and mutant peptide into its components.
Structural data indicate that protein level of the 3′ domain is proportional to its rigidity, displaying an apparent coupling between the binding of proteins and the assembly of the rRNA secondary elements.
These structures provide insights into the mechanism of neutralization, and the effect of various mutations on antibody affinity, and enable a comparison between the binding of the M18 antibody and CMG2 with PAD4.
No obvious binding mode difference was found between the binding of Z-ligands to MIF and P1G, which shows that this mutation does not have a significant affect on the binding of Z-ligands to P1G.
We demonstrated that the surface modification of adding an amino group to nSP70 weakens the binding of nSP70 to albumin, transferrin, and IgG, although there were no significant differences between the binding of nSP70 and that of nSP70 with the surface modification of an added carboxyl group (Figure 3A,B,C).
Previously, using cell-surface envelope glycoproteins derived from infection of a laboratory-adapted HIV-1 strain, a correlation had been established between the binding of gp120-directed antibodies to the viral glycoprotein and the ability of the antibodies to neutralize laboratory-adapted isolates.
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To investigate the relationship between transcription and the binding of EAST to chromosomes, we performed a run-on transcription assay by including BrUTP into detergent buffer.
Specifically, the relationships between the binding sites of one family of miRNAs and all of the mRNA sites must be elucidated.
Binding of a TF to a gene regulatory region requires a match between the binding sequence of the TF and the operator region of that particular gene.
Virtual screening of databases was carried out to identify novel compounds on the basis of difference between the binding pockets of the two proteins.
Using the best myogenin dataset, we found a high degree of overlap between the binding sites of the two factors.
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