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In particular, the properties of macromolecular assemblies of multiple proteins bound to DNA have not previously been investigated in detail.
We have performed computational structural analysis and present herewith some general features we have observed about macromolecular assemblies of multiple proteins bound to DNA.
The energy Z-scores for direct and indirect readouts (conformational energy) have more negative values for complexes with multiple proteins bound to DNA (Table 3 and Table S31).
We wanted to evaluate the differences between water mediated contacts at protein-DNA interfaces in protein∶DNA complexes (single proteins bound to DNA) and in protein∶protein∶DNA complexes (multiple proteins bound to DNA).
We have performed computational structural analyses on macromolecular assemblies of multiple proteins bound to DNA using a variety of different computational tools: PISA; PROMOTIF; X3DNA; ReadOut; DDNA and DCOMPLEX.
The free energy barrier of assembly dissociation (ΔGdiss, Table 3) is higher for complexes involving multiple proteins bound to DNA (MultiProteins∶DNA) than those involving only single protein-DNA complexes (SubMultiProteins∶DNA, SingleProtein∶DNA and SingleSameProtein).
Similar(53)
Distortion is significantly higher when multiple proteins bind to DNA.
However, the conformational change of the DNA upon protein binding is significantly higher when multiple proteins bind to it than is observed when single proteins bind.
In order to check if DNA structural deformation is higher when multiple proteins bind to DNA we performed computational structural analysis of DNA structures.
Here we reported that there are also further conformational changes to the structure of DNA which are induced when multiple proteins bind to it.
Footprinting studies of multiple hnRNP A1 proteins bound to the ssA7 locus showed discrete protection patterns, inconsistent with binding-induced unwinding of the RNA secondary structure.
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many proteins bound
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multiple sdAbs bound
multiple fluorophores bound
multiple proteins co-purified
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