Determining the mechanism by which proteins attain their native structure is an important but
difficult problem in basic biology. The study of protein folding is difficult because it involves …

Therapeutic proteins require correct disulfide bond formation for biological activity and
stability. This makes their manufacturing and storage inherently challenging since disulfide …

Active RNase glycoprotein from three pieces: The glycoprotein enzyme ribonuclease C,
which contains a complex saccharide N‐glycan, was synthesized by sequential native …

The study of disulfide‐bond‐containing proteins has advanced our understanding of the
mechanism (s) by which the majority of secretory and membrane‐bound proteins acquire …

Organocatalysts derived from diethylenetriamine effect the rapid isomerization of non-native
protein disulfide bonds to native ones. These catalysts contain a pendant hydrophobic …

Almost all therapeutic proteins and most extracellular proteins contain disulfide bonds. The
production of these proteins in bacteria or in vitro is challenging due to the need to form the …

The production of proteins using recombinant DNA technology often requires the use of in
vitro protein folding. In order to facilitate in vitro protein folding, a redox buffer is added to the …

Abstract Aktives RNase‐Glycoprotein aus drei Segmenten: Das Glycoprotein‐Enzym
Ribonuclease C mit einem komplexen nonasaccharidischen N‐Glycan wurde durch …

The isomerase efficacy of the oxidoreductase, protein disulfide isomerase (PDI), has been
examined by a simple method. Using this technique, the pH-dependence of relative …

In vitro protein folding of disulfide containing proteins is aided by the addition of a redox
buffer, which is composed of a small molecule disulfide and/or a small molecule thiol. In this …