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Energy minimization of the whole complex showed, as expected, that most of the template interactions are preserved in the MTB structure, except for HIS11, ARG139 and GLN255.
Similar(59)
Template-independent enzyme-DNA interactions are known as anchor site interactions and a subset of these are believed to confer telomerase with the property of repeat addition processivity.
All of these interactions are also present in at least one of the templates used to build the model, although none of them is conserved across all templates.
The interactions are disturbing.
Interactions are few.
Interactions are complex.
Hence, I believe that the concept of the enhancer as a template for weak protein interactions is alive and well, and yes, still a mystery.
Template-nanoparticle interaction was investigated using a Biacore X100 instrument (GE Healthcare, USA).
We interpret the short-lived, stochastic interactions to be promoter-specific but non-productive RPc and RPo, because no interactions were observed with templates containing a null promoter sequence (at frame rates of 12.5 Hz, Figure 3B) and similar short-lived interactions were observed in the absence of NTPs (single exponential T 0 ∼0.3 s, Figure 3D).
The structure's non-bonding interactions were qualified as good in both the model and the template.
Relative crosslinking frequencies for combinatorial interactions were calculated as the ratio of the amount of product detected with crosslinked DNA template to the amount of product obtained with non-crosslinked, control DNA templates [17], [30].
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