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関連する概念動画

Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

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.
Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Structure and Nomenclature of Thiols and Sulfides02:17

Structure and Nomenclature of Thiols and Sulfides

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...
Electrophilic Aromatic Substitution: Sulfonation of Benzene01:22

Electrophilic Aromatic Substitution: Sulfonation of Benzene

Sulfonation of benzene is a reaction wherein benzene is treated with fuming sulfuric acid at room temperature to produce benzenesulfonic acid. Fuming sulfuric acid is a mixture of sulfur trioxide and concentrated sulfuric acid.

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関連する実験動画

Updated: May 24, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

アスパルティック酸から得られた強力で多用途の二硫化物減少剤です.

John C Lukesh1, Michael J Palte, Ronald T Raines

  • 1Department of Chemistry, ‡University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

Journal of the American Chemical Society
|February 23, 2012
PubMed
まとめ

ディチオブチラミン (DTBA) は,ディスルファイド結合の減少においてディチオトリトロール (DTT) を上回る新しいディチオール反応剤です. DTBAは中性pHで反応性が向上し,生物学的用途に優れています.

科学分野:

  • バイオケミストリー バイオケミストリー
  • 有機化学 オーガニック・ケミストリー
  • 化学生物学 化学生物学とは

背景:

  • ディチオトリエトール (DTT) は,生物分子の二硫化物結合を減少させるための標準反応剤です.
  • DTTのチオール基は,陽子化による中性pHではほとんど反応しないので,有効性が制限されます.
  • 水溶液における二酸化硫化物結合を減少させる剤をより効果的に作る必要がある.

研究 の 目的:

  • DTTの優れた代替品として (2S) - 2 - アミノ - 1 - 4 - ディメルカプトブタン (ディチオブチラミンまたはDTBA) を導入し,特徴づけること.
  • DTBAのpKa値とジスルファイド・レドックス・ポテンシャルを含む化学的性質を評価する.
  • DTTと比較して,様々な分子におけるディスルファイド結合の減少におけるDTBAのパフォーマンスを評価する.

主な方法:

  • 大規模生産に適した高収率のステップを介してl-アスパルティック酸からDTBAの合成.
  • DTBAのチオールpKa値とジスルファイドリオックスポテンシャル (E°) の決定.
  • DTBAとDTTの比較研究は,小分子とタンパク質における二硫化物結合の減少を研究しています.

主要な成果:

  • DTBAは,l-アスパルティック酸から効率的に合成されました.

さらに関連する動画

High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
12:16

High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli

Published on: July 30, 2014

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

関連する実験動画

Last Updated: May 24, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
12:16

High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli

Published on: July 30, 2014

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

  • DTBAは,DTTよりも約1単位低いチオールpKa値を示し,中性pHで反応性を高めます.
  • DTBAは,小さな分子とタンパク質の両方に対して,DTTよりも迅速なディスルファイド結合減少運動を示した.
  • DTBAのアミノ群は,容易に分離および結合することを可能にします.

    • 結論:

    • DTBAは,水溶液中の二硫化物結合を減らすために,DTTよりも有効な反応剤です.
    • DTBAの改良された反応性と結合能力は,生化学および化学生物学アプリケーションの貴重なツールになります.
    • DTBAの合成は,大規模なプロセスに対応し,より広範な使用を容易にします.