The authors noticed that the term “intrachain disulfide” is erroneously used five times within this Review (three in main text, and once Figure 6 9, respectively). In fact, disulfide bonds described are interchain disulfides. Thus, word “intrachain” should read “interchain” on page 11213, left column, line 2, 5; 11214, right 25, 1; 11231, 3. Revised versions of Figures which contain corrected w...

The introduction of dynamic bonds in polymeric materials facilitates the emergence new functionalities, such as self-healing capacity. Understanding role molecular structure efficiency process is fundamental to design with improved features. Computational chemistry has emerged a valuable tool for characterization materials. In this work, computational used analyze observed capacity set disulfid...

Determination and location of cystine residues are essential to protein characterization since their disulfide bonds stabilize chainfolding and multichain structure responsible for physical and biological properties. Reduction with mercaptans, such as dithiothreitol, in dissociating solvents is the choice procedure for attaining disulfide cleavage, since other methods may cause undesirable side...

Plasma plasminogen is the precursor of the tumor angiogenesis inhibitor, angiostatin. Generation of angiostatin in blood involves activation of plasminogen to the serine protease plasmin and facilitated cleavage of two disulfide bonds and up to three peptide bonds in the kringle 5 domain of the protein. The mechanism of reduction of the two allosteric disulfides has been explored in this study....

Defensins, which are small cationic molecules produced by organisms as part of their innate immune response, share a common structural scaffold that is stabilized by three disulfide bridges. Coprisin is a 43-amino acid defensin-like peptide from Copris tripartitus. Here, we report the intramolecular disulfide connectivity of cysteine-rich coprisin, and show that it is the same as in other insec...

Multiply-charged peptide cations comprised of two polypeptide chains (designated A and B) bound via a disulfide linkage have been reacted with SO2-* in an electrodynamic ion trap mass spectrometer. These reactions proceed through both proton transfer (without dissociation) and electron transfer (with and without dissociation). Electron transfer reactions are shown to give rise to cleavage along...

A photosensitive plate based on sintered TiO2 nanoparticles has been developed to carry out in-source photo-induced reductions for cleavage of disulfide bridges using glucose as a hole scavenger during laser desorption ionization.

Reaction of [Pd(1R,2R-diaminocyclohexane)Cl(2)] with the oxidised form of the tripeptide glutathione ([gamma]-l-glutamyl-l-cysteinyl-glycine) in aqueous solution leads to reductive cleavage of the disulfide bond.