Structural characterization of alzheimer dna promoter sequences from the amyloid precursor gene in the presence of thioflavin t and analogs

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SUMMARY

This binding to the DNA may resultand in conformational changes addition to Aβbe aggregates, binding to DNA-specific sequences produces an increase in which could induced ThT by non-covalent_bonds, hydrophobic_interactions, hydrogen fluorescence. [16]. couldThT be induced by non-covalent hydrophobic_interactions, hydrogen_bonds, weak molecules consist of twobonds, aromatic moieties-N,N-dimethylaniline and a 3,6-divan der Waals forces, etc. The crystallization DNA oligonucleotide froma the promoter region of the APP aim was create a selectionaffecting of suitable co-crystallization gene, as to well as sequences thecomplexes expressionfor ofcrystallization the APP gene . . .

 



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