Dmitry I. Cherny

TL;DR: Different classes of experiments are reviewed and a distinction is drawn between experiments that monitor signals from a large number of proteins, one molecule at a time, from those that follow a single protein molecule over many individual cycles.

TL;DR: In this paper, the authors used transmission electron microscopy to analyze the specificity and the extent of DNA bending upon binding of full-length wild-type human tumor suppressor protein p53 and the p53 core domain (p53CD) encoding amino acid residues 94−312, to linear double-stranded DNA bearing the consensus sequence 5′-AGACATGCCTAGACAT-GCCT-3′ (P53CON).

TL;DR: The data presented here suggest that p53CD can form stable specific and non-specific complexes with supercoiled DNA molecules, albeit of variable multimeric organization.

TL;DR: This method is useful to quantify directly from microscopy techniques, such as electron or scanning force microscopy, the true bending angle, either intrinsic or induced by a ligand, and its associated flexibility at a given locus in any small DNA fragment.

TL;DR: It is argued that adhesion of DNA to a charged surface may lead to additional static bending (kinking) of approximately 5 degrees per dinucleotide step without impairing the dynamic behavior of the DNA backbone.