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The specific hydrogen bond interactions of the amino group belonging to the 4-aminopyridine with the free O2O′2 compartment of the Schiff base ligands led to various supramolecular architectures: rectangles, chains, and ladders.
Further, in silico point mutation of BAX-Lys21 to Glu21 resulted in structural change in BAX and showed reduced binding energy and hydrogen bond interactions of the selected ligands.
For both MHC classes, the conserved hydrogen bond interactions of the MHC with the peptide backbone contribute to high affinity binding for a large number of different peptides while interactions with the peptide side chains determine the characteristic binding specificity of each MHC allotype.
Most of the hydrogen bond interactions of the peptidyl inhibitor resemble the hydrogen bonding of rosmarinic acid with caspase-3.
It can be observed that most of the hydrogen bond interactions of the peptidyl inhibitor resemble the hydrogen bonding of rosmarinic acid with caspase-3 and 4(b)).
The Thr to Leu substitutions disrupt the binding of the ordered water to sbwAFP by removing the stabilizing hydroxyl side chain hydrogen bond interactions of the threonine residues.
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The selective responses of the tetrahedrons thus should be attributed to both the size-fitting of the cavities and the potential hydrogen bond interaction of the amide groups.
An additional hydrogen bond interaction of the piperidine nitrogen to Gly-888 also contributes to the binding affinity of 1e to PARP-1.
Molecular dynamics simulations illustrated that the more stable hydrogen bond interaction of the UA derivative 12e with Ser191 and stronger hydrophobic interactions with Val198, Phe463 than those of OA derivative 12b mainly led to their significantly different CETP inhibitory activity.
The W122H and W106Y variants were specially designed to mimic the hydrogen-bond interactions of the naturally occurring Trp residues.
Internal H-bond and non-H-bond interactions of the L-3 layer account for 54 % and internal C-2 chainteractionsofs of C molecules account for 13%% of E T,Σ.
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