The source of increased stability in proteins from organisms that thrive in extreme thermal
environments is not well understood. Previous experimental and theoretical studies have …

Metal centers in metalloproteins involve multiple metal–ligand bonds. The release of metal
ions from metalloproteins can have significant biological consequences, so understanding …

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 …

Proteins exhibit a remarkable structural plasticity and may undergo conformational changes
resulting in protein misfolding both in a biological context and upon perturbing …

Extreme thermostabilities of proteins can be achieved by binding co-factors to the protein
structures. For various α-amylases protein stabilization upon calcium binding is a well …

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 …

Iron–sulfur centers are widespread in living organisms, mostly performing electron transfer
functions, either in electron transfer chains or as part of multi-enzymatic complexes, while …

The conformational changes during refolding and unfolding of the dual-color β-subunit in R-
phycocyanin (R-PC) were monitored by the spectra, fluorescence anisotropy, and FRET. It …

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 …

Compartmentalization is an essential cellular mechanism that allows cells to create and
organize controlled microenvironments for specific metabolic pathways, increase their …