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To investigate how CcpA can bind to such diverse sequence motifs, we tried to identify contributions to binding selectivity.
There is emerging evidence that certain neurexins polymorphs may differentially bind to such ligands and presumably affect their trans-synaptic properties.
As the human orthologue of Woc, ZNF198, interacts with a series of transcriptional regulators [36] we would suggest that the Drosophila Woc protein can also bind to such transcriptional cofactors in an HP1c regulated manner.
However, a pressing question is how does the same PG that appears relatively resistant to significant changes in curvature bind to such a wide range of fibril diameters: The curvature of the collagen fibril surface changes markedly from the very small (<20 nm) fibrils in developing tissue to the large >250 nm fibrils in aged tissue [7].
Little is known about how CcpA can bind to such diverse cre sequences.
As such, it remains unclear how the conserved ankyrin repeats can bind to such a wide variety of protein targets.
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We present here crystal structures of IGF-I bound to such a hybrid primary binding site and of a ligand-free version of an IR αCT peptide bound to an IR L1 plus cysteine-rich domain construct (IR310.T).
Both Def11 500 and Def11 500/CUEm bound to such beads, but showed only background binding to the empty control beads.
The enzyme is covalently bound to such an electrode by activating the carboxy groups of the polymer.
If a therapeutic protein binds to such a receptor, it will be internalized as well and located in sorting endosomes at a pH of ∼6 [ 2].
Certain mannose-specific lectins, such as concanavalin A (ConA), can recognize N-linked glycans and bind to glycoproteins such as SUR1 [ 29].
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