Although protein-folding studies began several decades ago, it is only recently that the tools
to analyze protein folding at the single-molecule level have been developed. Advances in …

Conspectus Hemes are ubiquitous in biology and carry out a wide range of functions. The
heme group is largely invariant across proteins with different functions, although there are a …

Out-of-plane (OOP) deformations of the heme cofactor are found in numerous heme-
containing proteins and the type of deformation tends to be conserved within functionally …

Cytochrome (cyt) c is an important electron transfer protein. The ruffling deformation of its
heme cofactor has been suggested to relate to its electron transfer rate. However, there is no …

In order to understand the mechanism by which a polypeptide chain folds into its functionally
active native state it is necessary to characterize in detail all the species accumulated along …

The studies of the folding of structurally related proteins have proved to be a very important
tool for investigating protein folding. Here we review some of the insights that have been …

Discussing the role of metal ions in protein folding, this volume provides case examples of
protein folding and stability studies in particular systems as well as proteins that comprise …

The DNA binding domain (DBD) of p53 folds by a complex mechanism that involves parallel
pathways and multiple intermediates, both on-and off-pathway. This heterogeneity renders …

Protein dynamics is intimately linked to function. In metalloproteins, dynamics are often
coupled to redox activity, ligand binding and enzyme function. We provide a concise …

A unifying view has been recently proposed according to which the classical diffusion–
collision and nucleation–condensation models may represent two extreme manifestations of …