Recent advances in generating active proteins through refolding of bacterial inclusion body
proteins are summarized in conjunction with a short overview on inclusion body isolation …

Methods enabling the dechalcogenation of thiols or selenols have been investigated and
developed for a long time in fields of research as diverse as the study of prebiotic chemistry …

Self-assembled monolayers (SAMs) of alkane thiols on gold and other metals are versatile
constructs with which to study interfacial phenomena and reactions at surfaces. Surface …

A novel drug carrier with dual triggerable release properties based on keratin graft poly
(ethylene glycol)(keratin-g-PEG) copolymers is reported. Keratin-g-PEG copolymers with …

Dynamic combinatorial chemistry applied to biological environments requires the exchange
chemistry of choice to take place under physiological conditions. Thiol-disulfide exchange …

Impaired redox homeostasis in the endoplasmic reticulum (ER) may contribute to proinsulin
misfolding and thus to activate the unfolded protein response (UPR) and apoptotic …

Proteins form native structures through folding processes, many of which proceed through
intramolecular hydrophobic effect, hydrogen bond and disulfide-bond formation. In vivo …

We report the first example of a synthetic thiol-based compound that promotes oxidative
protein folding upon 1-equivalent loading to the disulfide bonds in the client protein to afford …

The efficiency of the protein refolding process lies in identification of the optimal conditions.
However, a number of challenges need to be overcome to achieve this. This review first …

A recurring obstacle for structural genomics is the expression of insoluble, aggregated
proteins. In these cases, the use of alternative salvage strategies, like in vitro refolding, is …