The general importance of the Fe‐S cluster prosthetic groups in biology is primarily
attributable to specific features of iron and sulfur chemistry, and the assembly and interplay …

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 …

Structural calcium sites control protein thermostability and activity by stabilizing native folds
and changing local conformations. Alicyclobacillus acidocaldarius survives in thermal-acidic …

Since the determination of the first molecular models of proteins there has been interest in
creating proteins artificially, but such methods have only become widely successful in the …

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 …

The specific arrangement of secondary elements in a local motif often totally relies on the
formation of coordination bonds between metal ions and protein ligands. This is typified by …

Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated
employing a toolbox of spectroscopic methods. FTIR and visible CD were used for …

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 …

Rieske proteins and Rieske ferredoxins are present in the three domains of life and are
involved in a variety of cellular processes. Despite their functional diversity, these small Fe …

Detailed structural models of di-cluster seven-iron ferredoxins constitute a valuable resource
for folding and stability studies relating the metal cofactors' role in protein stability. The here …