Multi-protein DNA replication complexes called replisomes perform the essential process of
copying cellular genetic information prior to cell division. Under ideal conditions, replisomes …

We review 50 years of use of 2′, 3′-O-trinitrophenyl (TNP)-ATP, a fluorescently tagged
ATP analog. It has been extensively used to detect binding interactions of ATP to proteins …

The RecBCD helicase initiates double-stranded break repair in bacteria by processively
unwinding DNA with a rate approaching∼ 1,600 bp· s− 1, but the mechanism enabling such …

DEAD-box proteins (DBPs) couple ATP utilization to conformational rearrangement of RNA.
In this chapter, we outline a combination of equilibrium and kinetic methods that have been …

Enzyme-catalyzed protein unfolding is essential for a large array of biological functions,
including microtubule severing, membrane fusion, morphogenesis and trafficking of …

Quantitative analysis of the interactions of the Escherichia coli primosomal PriB protein with
a single-stranded DNA was done using quantitative fluorescence titration, photocrosslinking …

Escherichia coli ClpB is a molecular chaperone that belongs to the Clp/Hsp100 family of
AAA+ proteins. ClpB is able to form a hexameric ring structure to catalyze protein …

The oligomerization reaction of the Escherichia coli DnaT protein has been quantitatively
examined using fluorescence anisotropy and analytical ultracentrifugation methods. In …

Elucidation of ligand-macromolecule interactions requires detailed knowledge of energetics
of the formed complexes. Spectroscopic methods are most commonly used in characterizing …

Allosteric interactions between the strong and weak nucleotide-binding sites and the total
and proper single-stranded (ss) DNA-binding sites of the Escherichia coli PriA helicase have …