Over the last decade, studies have unraveled many aspects of endogenous production and
physiological functions of carbon monoxide (CO). The majority of endogenous CO is …

To understand the mechanism of ionic detergent‐induced protein denaturation, this study
examines the action of sodium dodecyl sulfate on ferrocytochrome c conformation under …

Several studies have found millisecond protein folding reactions to be controlled by the
viscosity of the solvent: Reducing the viscosity allows folding to accelerate. In the limit of very …

We report molecularly imprinted polymers (MIPs) for selective adsorption of proteins using a
poly (ethylene glycol)(PEG)-based cross-linker with ionic monomers. To clarify the utility of …

Osmolytes are known to stabilize proteins under stress conditions. Thermal denaturation
studies on globular proteins (β-lactoglobulin, cytochrome c, myoglobin, α-chymotrypsin) in …

Metalloproteins account for over one-third of all proteins in nature and play important roles in
biological processes. The formation of the native structures of metalloproteins requires not …

Subdenaturing concentrations of guanidine hydrochloride (GdnHCl) stabilize proteins. For
ferrocytochrome c the stabilization is detected at subglobal level with no measured change …

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 …

The structural changes of ferrous Cyt-c that are induced by binding to SDS micelles,
phospholipid vesicles, DeTAB, and GuHCl as well as by high temperatures and changes in …

Proteins fold by diffusional motion, driven by molecular collisions but limited by frictional
drag. We then expect that the timescale of simple diffusional motions of the polypeptide …