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The elevated (or depressed) level of intracellular Ca2+ binding protein does not markedly affect gene expression.
Bovine mammary fatty acid binding protein does not appear to be glycosylated.
This suggests that this specific methyl-DNA binding protein does not have a major role in silencing the inactive X through histone modification.
This is the only known example of "silent" phosphorylation, that is, where phosphorylation of a Thr in the active site of an RNA binding protein does not result in a conformational change.
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The resulting purified ML protein was able to bind to amylose resin (Figure 5B) and could subsequently be eluted with maltose-containing buffer (Figure 5C), which showed that the covalent attachment of 5-carboxyfluorescein to the C-terminus of the maltose binding protein did not interfere with the protein's biochemical function.
Similarly RNAi knockdown of staufen (stau ), which encodes a double-stranded RNA binding protein, did not result in any overt dendritic defects whereas dendritic branching was reduced in stau mutant larvae (data not shown).
This chemokine-binding protein does not share any relevant sequence or structural homology to any other known proteins, notably the viral chemokine-binding proteins, and moreover, is considerably smaller, being only 10 kDa compared to the viral proteins which range in size between 30 40 kDa.
However, such a model would not easily explain why far more abundant hydrophobic binding proteins do not outcompete SRP, why SRP cannot bind those same sequences post-translationally, and how SRP can rapidly find these transient and rare species to prevent aggregation.
Sequence-specific nucleic acid binding proteins do not recognize one sequence out of all possibilities; rather, they bind to many sequences with a range of affinities.
What is surprising is that osmotin and adiponectin, the receptor binding proteins, do not share sequence similarity even if both have a similar internal beta-barrel domain [5].
Furthermore, the simultaneous addition of the ligands and binding proteins did not change migration behaviour (Supplementary Material, Fig. S9Da d).
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