Journal ArticleDOI
DNA-Protein Interactions
TLDR
This book is very referred for you because it gives not only the experience but also lesson, that's not about who are reading this dna protein interactions book but about this book that will give wellness for all people from many societies.Abstract:
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Journal ArticleDOI
Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice.
TL;DR: The results indicate that the binding of any non-interacting ligand covering more than one lattice residue results in non- linear (convex downward) Scatchard plots, and the introduction of positive ligand-ligand co-operativity antagonizes this non-linearity, and eventually leads to plots of the opposite curvature.
Journal ArticleDOI
Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity.
TL;DR: The purpose of this review is to examine the various effects of low- molecular-weight electrolytes on the associations and interactions of proteins and nucleic acids through general electrostatic effects rather than chemical effects of particular ions.
Journal ArticleDOI
Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication.
TL;DR: Evidence is provided here that the major pathway of induction after damage by a typical agent, ultraviolet light, requires an active replication fork; this result supports the model that DNA replication leaves gaps where elongation stops at damage-induced lesions, and thus provides the single-stranded DNA that activates RecA protein.
Journal ArticleDOI
Regulation of abscisic acid-induced transcription.
Peter Kamp Busk,Montserrat Pagès +1 more
TL;DR: Results have shown that cooperative action of cis-elements and the promoter configuraton is crucial for regulation by abscisic acid, and several elements are organ- and species-specific.
Journal ArticleDOI
Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism.
TL;DR: In this article, the crystal structures of the SRA domain of UHRF1 bound to DNA containing a hemi-methylated CpG site were described and the structures showed that methyl-cytosine is flipped out of the DNA helix and inserted into a binding pocket on the SSA domain.