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The use of XPS to probe the S2p binding energy was not possible due to the low sulfur loadings (as determined by elemental analysis), which resulted in the observed peak having poor signal-to-noise ratio.
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However, unlike the ground-state exciton, the first-excited binding energy is not a monotonically decreasing function of x Al 1 over the range of values of this quantity considered.
In this case the variation of binding energy is not symmetric, it has only a maximum value when the impurity is located at the center of QD1. Figure 2 The variations of binding energy in terms of impurity position in the presence of electric fields.
The absolute binding energies are not converged in these calculations; one may note in passing that the performance of the semiempirical PMO model for water is exceptionally good, but the main purpose here is to test the performance of many-body expansion theory.
The binding free energy was not significantly correlated to the molecular weight, KOA, BCF, t1/2, or IC50 when P was more than 0.05.
Since the extraction of the entropic contribution per-residue from the binding free energy was not available, hot spots were determined on the basis of the enthalpy terms.
However, it should be taken into account that in this case the enthalpy calculation using MOPAC is only performed for only one minimum with the lowest energy, but as it was mentioned before the lowest energy position has RMSD > 3 Å from the native ligand position in the protein for 2 ligands from 8. Entropic contribution of the binding free energy was not also taken into account in this case.
First, toxins can bind with relatively high affinity to their target channels because binding free energy is not 'spent' bringing about a protein conformational change.
It is also well known that the binding free energy is not uniformly distributed over the protein interfaces, and a small portion of interface residues contribute the most of binding free energy instead [ 11].
Our energy wasn't good.
Apparently, the binding energy is able to provide some but not all of the energy required to compensate for the destabilizing effect of the mutation.
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