Thermal denaturation-based methods are becoming increasingly used to characterize
protein stability and interactions. Recent technical advances have made these methods …

The role of metal ions in protein folding and structure is a critical topic to a range of scientists
in numerous fields, particularly those working in structural biology and bioinorganic …

Lactoperoxidase (LPO) belongs to the mammalian peroxidase family and catalyzes the
oxidation of halides, pseudo-halides and a number of aromatic substrates at the expense of …

The biological insertion of iron–sulfur clusters (Fe–S) involves the interaction of (metallo)
chaperons with a partly folded target polypeptide. In this respect, the study of nonnative …

Multiple-CoA dehydrogenase deficiency (MADD) is an inborn disorder of fatty acid and
amino acid metabolism caused by mutations in the genes encoding for human electron …

Addition of iron salts to chaotrope-denatured aporubredoxin (apoRd) leads to nearly
quantitative recovery of its single Fe (SCys) 4 site and native protein structure without …

A detailed understanding of the molecular basis of protein folding and stability determinants
partly relies on the study of proteins with enhanced conformational stability properties, such …

Iron-sulfur proteins are a multifaceted class of proteins containing iron-sulfur clusters (Fe-S)
as a prosthetic group. These proteins are ubiquitously found within all life domains and are …

S100B is a Ca 2+, Cu 2+ and Zn 2+-binding protein highly expressed in human brain, with a
intra and extracellular function. It is involved in several pathological processes in which …

Over the last few decades a large effort has been done in the structural biochemistry field.
This effort is based on the study of some proteins, namely metalloproteins, that contain …