Results 1 to 10 of about 54,679 (294)

A novel method for the mechanochemical synthesis of unsymmetrical disulfides using phosphorodithioic acid derivatives [PDF]

open access: yesScientific Reports
In this study, we report the efficient synthesis of unsymmetrical disulfides using a mechanochemical ball-milling approach. This research successfully yielded alkyl-alkyl, alkyl-aryl, and aryl-aryl unsymmetrical disulfides without any detectable ...
Mikołaj Walter   +4 more
doaj   +2 more sources

Photocatalytic Bilateral Disulfuration of Thioethers Toward α‐Sulfide Disulfides With Antibacterial Activity [PDF]

open access: yesAdvanced Science
α−Sulfide disulfides represent valuable motifs in organic and pharmaceutical chemistry. However, the limited availability of synthetic approaches for α−sulfide disulfides has impeded progress in this field.
Qingqiang Tian   +4 more
doaj   +2 more sources

Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols [PDF]

open access: yesAntioxidants
Thiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie   +3 more
doaj   +2 more sources

Synthesis of disulfides and 3-sulfenylchromones from sodium sulfinates catalyzed by TBAI [PDF]

open access: yesBeilstein Journal of Organic Chemistry
A new synthetic method for disulfides and 3-sulfenylchromones is reported. This innovative approach is based on the tetrabutylammonium iodide (TBAI)/H2SO4 reduction system using sodium sulfinate as key component, thus eliminating the need for thiols and ...
Zhenlei Zhang   +6 more
doaj   +2 more sources

Synthesis and Biological Activity of Unsymmetrical Monoterpenylhetaryl Disulfides

open access: yesMolecules, 2022
New unsymmetrical monoterpenylhetaryl disulfides based on heterocyclic disulfides and monoterpene thiols were synthesized for the first time in 48–88% yields.
Denis V. Sudarikov   +12 more
doaj   +1 more source

Identification of allosteric disulfides from labile bonds in X-ray structures [PDF]

open access: yesRoyal Society Open Science, 2018
Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed.
Aster E. Pijning   +4 more
doaj   +1 more source

The effect of tensile stress on the conformational free energy landscape of disulfide bonds. [PDF]

open access: yesPLoS ONE, 2014
Disulfide bridges are no longer considered to merely stabilize protein structure, but are increasingly recognized to play a functional role in many regulatory biomolecular processes.
Padmesh Anjukandi   +3 more
doaj   +1 more source

Visible Light‐Driven Photocatalytic Transformation of Thiols to Disulfides in Water Catalyzed by Bi2S3

open access: yesAdvanced Energy & Sustainability Research, 2023
Selective coupling of thiols to produce disulfides is one very important and classic type of coupling reactions. Herein, an environmentally friendly and practical photocatalytic system for oxidative coupling of thiols to disulfides is developed.
Fengyun Su   +8 more
doaj   +1 more source

Dipotassium 1,3,4-thiadiazole-2,5-bis(thiolate) as a new S-donor for direct synthesis of symmetrical disulfides

open access: yesScientific Reports, 2022
In this research, a simple, efficient and novel protocol is eveloped for the direct synthesis of symmetrical disulfides using dipotassium 1,3,4-thiadiazole-2,5-bis(thiolate) as a new, low toxicity, inexpensive, stable solid and free of foul-smelling ...
Mohammad Soleiman-Beigi   +3 more
doaj   +1 more source

Vicinal disulfide turns [PDF]

open access: yesProtein Engineering Design and Selection, 2003
The formation of a disulfide bond between adjacent cysteine residues is accompanied by the formation of a tight turn of the protein backbone. In nearly 90% of the structures analyzed a type VIII turn was found. The peptide bond between the two cysteines is in a distorted trans conformation, the omega torsion angle ranges from 159 to -133 degrees, with ...
Carugo, O.   +6 more
openaire   +4 more sources

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