[Structural organization of DNA complexes with proteins HMGB1 and HMGB1-(A+B)].
Copyright policy [Structural organization of DNA complexes with proteins HMGB1 and HMGB1-(A+B)].
The interaction between DNA and the nonhistone proteins HMGB1 and HMGB1-(A+B) has been studied using circular dichroism and scanning force microscopy. The recombinant protein HMGB1-(A+B) has no negatively charged C-terminal domain characteristic for HMGB1. Our earlier suggestion about the structural interaction of tandem HMGB1-domains of the recombinant protein with DNA was confirmed. It was shown that the C-terminal part modulates the interactions of HMGB1-domains with DNA. Without the C-terminal sequence, the HMGB1-(A+B) protein forms DNA-protein complexes with the ordered supramolecular structure.
Circular Dichroism, Microscopy, Electron, Scanning, Animals, Humans, Cattle, DNA, HMGB1 Protein, Recombinant Proteins, Protein Binding, Protein Structure, Tertiary
Circular Dichroism, Microscopy, Electron, Scanning, Animals, Humans, Cattle, DNA, HMGB1 Protein, Recombinant Proteins, Protein Binding, Protein Structure, Tertiary
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).0 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Average impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!