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A divalent chemical group consisting of two sulfur atoms, or a compound in which it is combined with other elements or groups. Also called bisulfide.


(Elements & Compounds) a variant spelling of disulphide


(daɪˈsʌl faɪd, -fɪd)

1. (in inorganic chemistry) a sulfide containing two atoms of sulfur, as carbon disulfide, CS2.
2. (in organic chemistry) a sulfide containing the bivalent group −SS−, as diethyl disulfide, C4H10S2.
References in periodicals archive ?
2015) Extracellular disulfide bridges stabilize TRPC5 dimerization, trafficking, and activity.
Oxidant sensing by reversible disulfide bond formation.
4-2a-b-c-d-e)/2] contained in a quantity from 1 to 20 mass % relative to the quantity of silica; and a thiuram disulfide vulcanization accelerator contained in a quantity from 0.
The major aroma-active compounds in milks were hydrogen sulfide, dimethyl sulfide, 2-butanone and furfural in DSI-UP-treated milks; diacetyl, 3-methyl butanal, dimethyl disulfide, methional and benzaldehyde in IND-UP-treated milks; and carbon disulfide, 1-octen-3-one and 1-octen-3-ol in HTST-treated milks, respectively.
Here, the authors report on the large-scale, spatially controlled synthesis of heterostructures made of single-layer semiconducting molybdenum disulfide contacting conductive graphene.
Thiols engage in oxidation reactions with oxidant molecules, forming disulfide bonds.
Our reason for asking dates back to the use of molybdenum disulfide in an oil additive as a friction reducer in car racing engines.
Another approach for intrinsic self-healing is by means of the formation of covalent bonds that allow chain exchange reactions such as the dynamic reversible formation of acylhydrazones [11], trithiocarbonates reshuffling [12], the reaction exchange of siloxane segments [13, 14], and the metathesis reaction of disulfide bonds [15-17].
The Protein Disulfide Isomerase (PDI) is a family of thiol isomerases originally found in the endoplasmic reticulum (ER) that were later discovered in the cytosol and surface of endothelial cells and platelets, among others [13, 14].
Changes of expression conditions were insufficient for soluble expression of reteplase in SHuffle T7 as a genetically engineered host for production of disulfide bonded proteins.
The hypothesis therefore is that the oxidation and reduction of disulfide bonds present in lactoferrin, which determine protein structure, is the mechanism through which lactoferrin exhibits its antimicrobial property.
The work underscores how materials properties change at the nanoscale, since bulk molybdenum disulfide does not exhibit piezoelectric properties.