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Reversible oxygen binding is the main function of haemoglobin: it results from equilibrium between two quaternary states: the first is a relaxed one, which displays a high oxygen affinity while the second is a tense one with low affinity.
Thus, our results suggest that α-Syn's membrane binding is the main cause of the inhibition of SNARE-dependent lipid mixing.
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It is interesting to observe that oxidative processes, hydrolase activity and nucleic acid binding are the main processes represented and most were already pointed out as having influence during resistance to microorganisms (Table 2).
These results clearly indicate that the in vivo pharmacokinetics and biodistribution of the targeted and non-targeted nanoparticles are comparable; and thus, VEGFR specific binding was the main factor responsible for enhanced tumor uptake of Cu-NOTA-MSN-PEG-VEGF121 over Cu-NOTA-MSN-PEG.
The main issue with variable binding is the possibility of variable capture in substitutions.
Accordingly, the reverse pattern of binding was observed for these compounds: the main feature of their binding is the interaction with aromatic amino acids in the S4 pocket.
CDR3 is the TCR motif that directly binds MHC-presented peptide epitopes and this binding interaction is the main factor conferring T cell antigen specificity.
The V3 loop of human immunodeficiency virus type 1 (HIV-1) is critical for coreceptor binding and is the main determinant of which of the cellular coreceptors, CCR5 or CXCR4, the virus uses for cell entry.
Finally, vitamin D-binding protein is the main carrier for vitamin D and its metabolites, known to be essential in the development, function, and maintenance of healthy bones through the regulation of calcium homeostasis (Speeckaert et al. 2006).
Vitamin D binding protein (DBP) is the main transporter of vitamin D in the bloodstream.
H+ transfer to Asp116 and Na+ binding to Asn112 is the main process for the formation of the (L/)M and O states, respectively.
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CEO of Professional Science Editing for Scientists @ prosciediting.com