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The mechanisms by which intrinsically disordered proteins engage in rapid and highly selective binding is a subject of considerable interest and represents a central paradigm to nuclear pore complex (NPC) function, where nuclear transport receptors (NTRs) move through the NPC by binding disordered phenylalanine-glycine-rich nucleoporins (FG-Nups).
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The role of membrane lipid charges in the Penetratin binding has been a subject of controversy.
The telomere-binding properties may also be a subject of rapid adaptive coevolution of function as occurs with another essential structure, centromeric repeats and specific centromeric histone types (Malik and Henikoff 2001).
The kinetic structural transitions revealed by these studies rely on conformational flexibility whose thermodynamic contribution to cooperative ligand binding is the subject of this study.
Receptor expression measured by ligand binding is not subject to such error; using such techniques, pancreatic adenocarcinomas did not express GLP-1 receptors (6).
However, it must be pointed out that there may be a risk that this model will fail to exclude a possible antiendotoxin effect if endotoxin aminoglycoside binding is subject to saturation kinetics and if a lower endotoxin dose is used.
Notch proteins are membrane-bound receptors, that upon ligand binding, are subjected to cleavage by gamma-secretase, releasing an intracellular domain (N-ICD) directly involved in transcriptional control (Ranganathan et al, 2011).
Selective binding of coordinating agents (cisplatin) to target molecules (DNA) and the contribution of H-bonding, electrostatic interactions, and steric effects in such binding are fundamentally important subjects.
The exact binding mechanism is still a subject of research [ 46].
[11C](R -PK11195 binding was examined in six contR -PK11195ts at two separate occasions, 6 weeks apart.
It has been suggested that this is through interference with the TLR4/MyD88/TIRAP complex [ 23- 27], however the exact binding partner of BtpA is still a subject of controversy.
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