Glutathione transferases (GSTs) are important detoxifying enzymes that catalyze the
conjugation of electrophilic substrates to glutathione. In recent years, GSTs have been of …

Electrophilic products of lipid peroxidation are important contributors to the progression of
several pathological states. The prototypical α, β–unsaturated aldehyde, 4-hydroxynonenal …

The catalytic activity of human glutathione S‐transferase A1‐1 (hGSTA1‐1), a homodimeric
detoxification enzyme, is dependent on the conformational dynamics of a key C‐terminal …

Recent advances in site-directed Cu2+ labeling of proteins and nucleic acids have added
an attractive new methodology to measure the structure-function relationship in …

Protein structures are classically described as composed of two regular states, the α-helices
and the β-strands and one non-regular and variable state, the coil. Nonetheless, this simple …

Glutathione transferases (GSTs) from the tau class (GSTU) are unique to plants and have
important roles in stress tolerance and the detoxification of herbicides in crops and weeds. A …

Combining rigid Cu (II) labels and pulsed-EPR techniques enables distance constraint
measurements that are incisive probes of protein structure and dynamics. However, the …

Abstract Nitroxide-and Cu 2+-based electron spin resonance (ESR) are combined to provide
insight into the conformational states of the functionally important α-helix of the human …

Human glutathione transferase A1-1 is a well studied enzyme, but despite a wealth of
structural and biochemical data a number of aspects of its catalytic function are still poorly …

Cytosolic GSTs (glutathione transferases) are a multifunctional group of enzymes widely
distributed in Nature and involved in cellular detoxification processes. The three …