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We show through mutagenesis and analysis of recombinant striated muscle α-tropomyosins that primary actin binding sites have a destabilizing coiled-coil interface, typically alanine-rich, embedded within a non-interface recognition sequence.
However, van Nimwegen et al. [10] (supporting text) use a simple maximum-entropy argument to show that the additivity assumption on energy does imply the PWM model for binding sites, if one also makes the reasonable assumption that binding sites have a significantly higher expected binding energy than random sites.
Consensus motifs constructed from too few binding sites have a low predictive value [ 37].
This work showed that pair binding sites have a monophyletic origin.
We found that the binding sites have a different rate of evolution at nucleosome occupied and depleted regions.
The inferred high confidence C/EBPα and PPARγ binding sites have a smaller overlap of 36%, compared with the previously reported >60% [ 16].
Similar(49)
Overall, 5% of human TF binding sites have an allelic imbalance in occupancy.
Targets with multiple (prerequisite or allosteric) binding sites have an increasing importance in drug design.
Type IA binding sites has an almost equal affinity for PACAP38, whereas type IB binding sites has a considerably greater affinity for PACAP38 than for PACAP27 [9].
This is in contrast to a similar study that found 3-43-4% p53 binding sites having a half site [ 54].
This second class of binding sites has a lower affinity (10 to 10 M−1) than the main binding site but n can vary substantially, from 2 to 24.
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