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Because aminopyridazine is a privileged structure in neuropharmacology, we determined the high-resolution crystal structure of a binary complex between the kinase domain and a molecular fragment of the DAPK inhibitor.
The proposed method is based on the formation of a binary complex between the studied drugs and eosin Y in aqueous buffered medium (pH 3.5).
These reactions include the formation of a binary complex between the metal and mono-deprotonated ascorbic acid molecule, and dioxygen coordination by the bound metal.
In contrast to Kf-exo–, the binding in the binary complex between the modified template and pol β is less tight than that in the complex containing the unmodified template, where the differences in binding are approximately 3-fold for FABP and 5- to 6-fold for FAAF, respectively.
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The method suggested is devoted to study the formation of a binary complex between each of the studied drugs and eosin Y in an attempt to develop a simple, sensitive and accurate extraction- free spectrophotometric method for the determination of the studied drugs in their pharmaceutical preparations.
Thus we have demonstrated a binary complex between dystroglycan and the Tks5 SH3 domain in vitro, and by GST-affinity chromatography demonstrated that dystroglycan from cell extracts can also bind the Tks5 SH3 domain, but in the cellular context the dystroglycan recovered on these columns appears to be phosphorylated on Y890.
To obtain crystals of the binary complex between MTase and 5'-capped RNA, the biotinylated 5'-capped RNA octamer with the sequence 5'-GpppAGAACCUG-biotin-TEG-3' [23] was co-crystallized with 4 mg/mL of DENV-3 MTase with a molar ratio of 1.7∶1 using the hanging drop vapour diffusion method.
Comparison of the KIX·MLL and KIX·MLL·pKID complexes with the binary complex between KIX and PCET reveals a slight difference in the orientation of the bound ligand peptide PCET versus MLL.
Sec17 did not associate with, or impede formation of, binary complexes between Sly1 and the N-peptide of full-length Sed5.
In the crystal structure of the covalent enzyme DNA binary complex the distance between the DNA O5′ and the Nζ Lys, that is considered the proton acceptor site, is 7.2 Å [ 4, 6].
Structural studies of binary complexes between Escherichia coli TS and various nucleotides suggest the chemotherapeutic agent FdUMP and the natural ligand dUMP bind similarly.
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