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 …

The process by which small proteins fold to their native conformations has been intensively
studied over the past few decades. The particular chemistry of disulfide-bond formation has …

The structural characterization of proteins expressed from the genome is a major problem in
proteomics. The solution to this problem requires the separation of the protein of interest …

In organic molecules a divalent sulfur atom sometimes adopts weak coordination to a
proximate heteroatom (X). Such hypervalent nonbonded S··· X interactions can control the …

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

Since the finding that selenium is an essential micronutrient for our life as well as the
discovery of selenocysteine (Sec) as the twenty-first proteinogenic amino acid that is …

Prion protein (PrP) is the major component of the partially protease-resistant aggregate that
accumulates in mammals with transmissible spongiform encephalopathies. The two …

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 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 …

Abstract β2-Microglobulin (β2M), the light chain of the type I major histocompatibility
complex, is a major component of dialysis-related amyloid fibrils. β2M in the native state has …