Disulfide bonds play an important role in understanding protein folding, evolution, and in studies related to determining structural and functional properties of specific proteins. At the state-of-the-art, a large number of computational techniques have been proposed for determining disulfide bonds. Operating across the gamut of input data, from pure sequence-based information to spectra from m...

Disulfide bond formation drives protein import of most proteins of the mitochondrial intermembrane space (IMS). The main components of this disulfide relay machinery are the oxidoreductase Mia40 and the sulfhydryl oxidase Erv1/ALR. Their precise functions have been elucidated in molecular detail for the yeast and human enzymes in vitro and in intact cells. However, we still lack knowledge on ho...

Disulfide bonds generally show only limited cleavage in positive ion mode collision activated dissociation (CAD). However, it has been emonstrated that a reverse situation exists in negative ion mode in which preferential S S and C S bond cleavage occurs. Here, we show that lectron detachment dissociation (EDD) and infrared multiphoton dissociation (IRMPD) of peptide anions containing disulfide...

The proteins PomA, PomB, MotX, and MotY are essential for the motor function of Na+-driven flagella in Vibrio spp. Both MotY and MotX have the two cysteine residues (one of which is in a conserved tetrapeptide [CQLV]) that are inferred to form an intramolecular disulfide bond. The cysteine mutants of MotY prevented the formation of an intramolecular disulfide bond, which is presumably important...

Macrocyclic peptides with multiple disulfide cross-linkages, such as those produced by plants and those found in nonhuman primates, as components of the innate immunity, hold great promise for molecular therapy because of their broad biological activities and high chemical, thermal, and enzymatic stability. However, for some, because of their intricate spatial arrangement and elaborate interstr...