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Exact(12)
Around the interaction point, about 300 m of both rings were completely redesigned for the new collision scheme.
Azosalicylic acids with two hydroxy groups, either in the para position of both rings or in the ortho position of one ring and para position of the other, gave rise to well defined oxidation peaks at significantly less positive potentials.
Studies of the variation in chemical shift anisotropy indicate an increase in oscillations of both rings about the chain axis, with increasing temperature, and these motions appear not to be coupled with the motion of the carbonyl group.
For the compounds with the hydroxyl groups in the para position of both rings, rereduction waves were also seen on the return scan, indicating that the oxidation products were stable on the voltammetric time scale.
The electronic effect of the substituents in the ortho-position as well as the total electronic effect of both rings on the electrochemical potential values was estimated using the linear fit for the relationship between EOx1/2+ERed1/2 vs. the sum of Hammett constants (σp + σo·cosθ).
The water was filled at the same level of both rings.
Similar(48)
One has the characteristic appearance of a both-ring open conformation (Supplementary Figure S1A) while the other shows a unique twisted pattern of all the subunits (Supplementary Figure S1B).
We demonstrated that the spatial distribution of both ring-shaped and smoothly varying circular slip distributions can be reproduced by the same method.
These data demonstrated a crucial role of the substitution position of the quinoline ring in this series of compounds and the contribution of both ring and terminal triple bond to the protective effect whereas the neuritogenic activity seemed to be mainly due to the presence of the lateral hydroxylated chain.
Removal of both ring nitrogen atoms of 1 (EC50: 0.08 μ m) to give 47 (EC50: 10 μ m) resulted in a 100-fold loss of activity, indicating that one or both of the pyrazine nitrogen atoms are important.
In addition to the interaction of both RING domains with E2 enzymes, the RBR of Parkin also interacts non-covalently with ubiquitin during chain formation (Chaugule et al, 2011).
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com