Disulfide bonds (–S–S–) are commonly present in biomolecules and have also been detected in astrophysical environments. In this work, the stability of the disulfide bond towards double ionization is investigated using ...

CueP confers bacterial copper resistance in the periplasm, particularly under anaerobic conditions, through an unknown mechanism. The only available structure and limited solution data suggest that CueP forms noncovalent ...

In order to study the stability of the disulfide chemical bond in molecules subjected to a flux of high energy photons, the ionic fragmentation of two molecules containing a disulfide chemical bond, dimethyl disulfide ...

Thiol-disulfide exchange reactions are highly reversible, displaying nucleophilic substitutions mechanism (S(N)2 type). For aliphatic, low molecular thiols, these reactions are slow, but can attain million times faster ...

The surprisingly rich chemistry of mechanically activated cleavage of disulfide bonds has been uncovered only recently. Using a disulfide protein mimic together with Cleland's reagent (DTT) as the attacking nucleophile in ...

Recombinant wild-pyrazinamidase from H37Rv Mycobacterium tuberculosis was analyzed by gel electrophoresis under differential reducing conditions to evaluate its quaternary structure. PZAse was fractionated by size exclusion ...

The control of the connectivity between nodes of synthetic networks is still largely unexplored. To address this point we take advantage of a simple dynamic chemical system with two exchange levels that are mutually connected ...

BACKGROUND: Human sperm nuclear decondensation in vivo involves protamine disulfide bond reduction by glutathione (GSH) and protamine/histone exchange, presumably with heparan sulfate (HS) as the protamine acceptor. The ...

High-resolution photoemission spectroscopy is used to characterize adlayers of ethane-, hexane-, and nonanedithiol molecules grown on Au(111) surfaces by the immersion method. The effect of using a reducing agent during ...