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Based on binding preference and sequence homology, the Eph receptors have been divided into two subclasses, EphA (A1 A8) and EphB (B1 B6) (Gale et al, 1996).
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There has been tremendous interest in developing in silico models for predicting nucleosome distributions based on DNA sequence composition and nucleosome binding preferences and the exclusionary effects of stiff DNA sequences that resist bending, such as poly dA-dT) tracts.
The final binding preference of each TF is made by taking a vote among these six binding preferences, and again in case of a tie random binding preference is assigned.
This result is consistent with the commonly accepted notion that structurally related TFs may have similar binding preference to DNA sequences, since the hierarchical clustering performed was solely based on the binding preference information (PFMs).
The nucleotide sequences of observed binding sites generally display a considerable variation, which may cause difficulties in the description of binding preferences using sequence motifs.
However, compared to H-pin 3e, tetraamide H-pin 5 demonstrated superior binding preference for the cognate sequence over its non-cognates, ACCGGT and AAATTT.
The results are used to determine drug binding sites and sequence preference, as well as conformational changes due to drug DNA interactions.
To take this possibility into account, a more sophisticated assumption can be applied; that is, TFs can have different binding preferences to different sequences or under different experimental conditions.
The dissociation constants indicate that Sp1ZF6(Arg)8 has an obvious DNA binding preference to discontinuous target sequences but not Sp1ZF6(Gly)10.
Our approach, based on the experimental data set of Tonikian et al. [7] profiling single-mutant PDZ binding specificities, aimed at generalizing the effects of single point mutations on binding preference to multi-mutant sequences.
The Lsm1-7-Pat1 complex has the binding preference for a U-rich sequence, and an in vitro analysis shows that the complex only binds to U20 but not other 20-mer homo-oligoribonucleotides. To compare the homo-oligomeric RNA-binding ability of Lsm2-3-Pat1C and Lsm1-7-Pat1C, fluorescence anisotropy assay was performed.
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