Disulfide containing

There are two manganese(II) sulfides, MnS and MnS2. Manganese(II) disulfide contains a S—S bond and has a pyrite stmcture. When a solution of a manganous salt is treated with ammonium sulfide, a flesh-colored hydrated precipitate is formed which is comprised of MnS and Mn(II)S2. This mixture very slowly changes to the mote stable green-black MnS. 

Figure 6.8 Schematic diagram of the enzyme DsbA which catalyzes disulfide bond formation and rearrangement. The enzyme is folded into two domains, one domain comprising five a helices (green) and a second domain which has a structure similar to the disulfide-containing redox protein thioredoxin (violet). The N-terminal extension (blue) is not present in thioredoxin. (Adapted from J.L. Martin et al.. Nature 365 464-468, 1993.)...

Loo, J. A. Edmonds, C. G. Udseth, H. R. Smith, R. D. Effect of reducing disulfide-containing proteins on electrospray ionization mass-spectra. Anal. Chem. 1990, 62, 693-698. 

Dissolve a disulfide-containing protein or peptide at a concentration of l-10mg/ml in 6M guanidine hydrochloride, 0.01 M sodium phosphate, 0.15 M NaCl, pH 7.4. Alternative... 

Protocol for Partial Reduction of Protein Disulfides or for Cleaving Disulfide Containing Modification Reagents... 

Figure 7.26 Dendrimers made with a disulfide-containing core can be reduced to produce dendrons having free thiol groups for surface modification. Dative binding of these thiol-dendrons to gold or metallic surfaces can provide a high density of amine groups for coupling proteins or other molecules.

Two Molecules Conjugated with a Disulfide-Containing Cross-linking Agent... 

Figure 8.1 Cleavage of disulfide-containing crosslinking compounds can be done using a reducing agent such as DTT. Reduction causes the conjugates to break apart into their original components with each component containing a portion of the crosslinker that terminates in a thiol group.

Epicorazine C - disulfide containing diketopiperazine with antimicrobial activity... 

Air Adsorption onto charcoal desorption with carbon disulfide, containing internal standard if desired GC/FID (NIOSH method 1003) 0.7 mg/m for 15 L sample 97 at 120-493 mg/m NIOSH 1994... 

Fig. 9.1 Tethering schematic. A fragment will be selected if it has inherent affinity for the protein and binds in the vicinity of the cysteine residue. An example disulfide-containing fragment is shown below, illustrating the variable portion, the linker, and the cysteamine piece that is lost when the fragment forms a disulfide bond with the protein.

Figure 1.5 Disulfide-containing receptors for peptides prepared by Hioki and Still.

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