Thiol Group
Thiol Group - Related Videos
02:33
Preparation and Reactions of Thiols
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2023
Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol. This reaction fails because the thiol product can undergo a second nucleophilic substitution reaction in the presence of an excess alkyl halide to generate a sulfide as a by-product. This limitation can be overcome by using thiourea as the nucleophile. The reaction first produces an alkyl...
11:17
Synthesis of Programmable Main-chain Liquid-crystalline Elastomers Using a Two-stage Thiol-acrylate Reaction
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Cited by 107 •
2016
A novel methodology is presented to synthesize and program main-chain liquid-crystalline elastomers using commercially available starting monomers. A wide range of thermomechanical properties was tailored by adjusting the amount of crosslinker, while the actuation performance was dependent on the amount of applied strain during programming.
02:17
Structure and Nomenclature of Thiols and Sulfides
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2023
Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry, similar...
12:07
Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
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Cited by 50 •
2012
Reactive oxygen species level is elevated when cells encounter stress conditions. Here we show the example of 3'-3' diaminobenzidine staining as well as cysTMT labeling and mass spectrometry to profile the redox proteome in Pseudomonas syringae treated tomato leaves.
11:25
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Cited by 1 •
2017
Biochemical and structural analyses of glycosylated proteins require relatively large amounts of homogeneous samples. Here, we present an efficient chemical method for site-specific glycosylation of recombinant proteins purified from bacteria by targeting reactive Cys thiols.
FAQs
The sulfur atom gives thiol-containing molecules three chemically important options: it can attack as a nucleophile, release a proton, or participate in oxidation. Nucleophilic behavior supports bond-forming reactions, proton donation contributes acid-base behavior, and oxidation links two thiol groups through a disulfide. These distinct pathways explain their broad synthetic and biological utility.
Oxidation couples two thiol groups to form a disulfide bond, creating a connection between sulfur-containing molecular sites. Because disulfide formation can be reversible, it provides a chemical link between molecular structure and redox processes. This behavior is especially important when researchers examine changes in protein structure or regulate sulfur-based chemical transformations.
Compared with an alcohol hydroxyl group, a thiol group is its sulfur analog, so the comparison helps chemists organize related functional-group chemistry. Yet the sulfur-containing site supports nucleophilic attack, proton donation, and oxidation to disulfides, giving it a distinct reaction profile within organic and biological chemistry.
In pharmaceutical chemistry, thiol reactivity contributes to the synthesis of sulfur-containing molecular structures and to transformations used when developing drug-related compounds. The important point is not a single application, but the availability of several reaction pathways, including nucleophilic behavior and oxidation. This flexibility connects basic sulfur chemistry with practical compound synthesis.
In protein chemistry, oxidation of thiol-containing sites can create disulfide bonds between parts of or among protein molecules. Those linkages help stabilize protein structure, while their reversible behavior connects structural changes with redox regulation. Consequently, thiol chemistry helps explain how sulfur-containing sites can influence both protein architecture and biological redox-related processes.
Thiol-based chemistry extends beyond small-molecule synthesis into polymers and surface-bound materials. In these settings, sulfur-centered reactions provide a chemical basis for constructing or modifying larger material systems, while analytical and biomedical uses apply the same reactivity in research contexts. This range connects functional-group chemistry with engineered materials and biological investigation.