Disulfide bonds between the side chains of cysteine residues are the only common crosslinks in proteins. Bovine pancreatic ribonuclease A (RNase A) is a 124-residue enzyme that contains four interweaving disulfide bonds (Cys26-Cys84, Cys40-Cys95, Cys58-Cys110, and Cys65-Cys72) and catalyzes the cleavage of RNA. The contribution of each disulfide bond to the conformational stability and catalyti...

A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection. The disulfide bonds in both proteins are cleaved at the cell surface by the small redox protein, thioredoxin. The target gp120 disulfide and its mechanis...

Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking protein disulfide isomerases (PDIs) can use alternative mechanisms for correct disulfide bond formation. By linking correct disulfide bond formation to antibiotic resistance, we selected mutants that catalyze correct disulfide formation in the absence of DsbC, Escherichia coli's PDI. Most of our mut...

Despite its exceptional optical absorptivity, suitable band gap, and earth abundance, the low open-circuit voltage of pyrite FeS2 has remained the biggest challenge preventing its use in photovoltaic devices. Two widely-accepted causes are: (i) Fermi level pinning caused by intrinsic surface states that appear as gap states; (ii) presence of the polymorph marcasite. Based on density-functional ...

in this article, we describe a photosensitizer (ps) whose ability to generate singlet oxygen (1o2) and fluorescence emission has been designed as tumor responsive. more specifically, the ps consists of a silicon phthalocyanine (sipc) core, axially substituted with two subphthalocyanine (subpc) units, covalently linked by a disulfide linker, which is cleavable in the presence of a strong reducin...

The Front Cover shows the bioconjugation of an antiproliferative prochelator to serum albumin via formation a disulfide bond with reduced cysteine on protein. abundance in blood is represented by red background featuring cells. disulfide-masked prochelators this class have activities at submicromolar levels panel cancer cell lines. design Matthew W. Lluis. More information can be found Communic...

Disulfide-rich domains are small protein domains whose global folds are stabilized primarily by the formation of disulfide bonds and, to a much lesser extent, by secondary structure and hydrophobic interactions. Disulfide-rich domains perform a wide variety of roles functioning as growth factors, toxins, enzyme inhibitors, hormones, pheromones, allergens, etc. These domains are commonly found b...

The active site cysteine of pig liver thioltransferase was identified as Cys22. The kinetics of the reaction between Cys22 of the reduced enzyme and iodoacetic acid as a function of pH revealed that the active site sulfhydryl group had a pKa of 2.5. Incubation of reduced enzyme with [1-14C]cysteine prevented the inactivation of the enzyme by iodoacetic acid at pH 6.5, and no stable protein-cyst...

Herein we present a significant step towards next-generation disulfide stapling reagents. A novel class of reagent has been designed to effect both disulfide reduction and functional re-bridging. The strategy has been applied to great success across various peptides and proteins. Moreover, application to a multi-disulfide system resulted in functional re-bridging without disulfide scrambling.