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In our Type I model, interactions are pairwise, while the Type II model allows each condensin binding site to interact with up to two others.
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Unexpectedly, Crm1 forms a dimer with an extensive interface that enhances association with Rev-RRE and poises NES binding sites to interact with a Rev oligomer.
This requires that some proteins have more than one binding sites to simultenaously interact with several protein partners.
Hence, binding sites present on the linker DNA are largely the active binding sites available to interact with the proteins to form protein complexes.
It appears that OTULIN has evolved Met1-linkage-specific Ub-binding sites to specifically interact with linear chains.
In the Type II model, each condensin binding site can interact with up to two others, thereby allowing the formation of higher order condensin binding site assemblies.
We have also demonstrated that p48v-myb can recognize a single consensus myb binding site and appears to interact with DNA as a protein monomer.
The availability of the binding site of nucleophosmin/B23 to interact with tumour suppressor is the basis for the cells being abnormal and resistant to induction of differentiation and apoptosis.
This observation inspired them to set up a metal constraint in Glide, which requires that a ligand atom lies within a certain region of the binding site in order to interact with specific target functionalities.
In our Type I model, each condensin binding site can interact with exactly one other site at a time, thus leading to stochastic pairwise interactions between chromatin segments.
A target might possess more than one binding sites, and each binding site might interact with several ligands.
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