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Related Concept Videos

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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Related Experiment Video

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

A potent, versatile disulfide-reducing agent from aspartic acid.

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
Summary
This summary is machine-generated.

Dithiobutylamine (DTBA) is a novel dithiol reagent that outperforms Dithiothreitol (DTT) in reducing disulfide bonds. DTBA offers enhanced reactivity at neutral pH, making it superior for biological applications.

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

Related Experiment Videos

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

Area of Science:

  • Biochemistry
  • Organic Chemistry
  • Chemical Biology

Background:

  • Dithiothreitol (DTT) is the standard reagent for reducing disulfide bonds in biological molecules.
  • DTT's thiol groups are largely unreactive at neutral pH due to protonation, limiting its efficacy.
  • There is a need for more effective disulfide bond reducing agents in aqueous solutions.

Purpose of the Study:

  • To introduce and characterize (2S)-2-amino-1,4-dimercaptobutane (dithiobutylamine or DTBA) as a superior alternative to DTT.
  • To evaluate DTBA's chemical properties, including its pKa values and disulfide redox potential.
  • To assess DTBA's performance in reducing disulfide bonds in various molecules compared to DTT.

Main Methods:

  • Synthesis of DTBA from l-aspartic acid via high-yielding steps suitable for large-scale production.
  • Determination of DTBA's thiol pKa values and disulfide redox potential (E°').
  • Comparative studies of DTBA and DTT in reducing disulfide bonds in small molecules and proteins.

Main Results:

  • DTBA was synthesized efficiently from l-aspartic acid.
  • DTBA exhibits thiol pKa values approximately 1 unit lower than DTT, enhancing reactivity at neutral pH.
  • DTBA demonstrated faster disulfide bond reduction kinetics than DTT for both small molecules and proteins.
  • The amino group of DTBA allows for facile isolation and conjugation.

Conclusions:

  • DTBA is a more effective reagent than DTT for reducing disulfide bonds in aqueous solutions.
  • DTBA's improved reactivity and conjugation capabilities make it a valuable tool for biochemical and chemical biology applications.
  • The synthesis of DTBA is amenable to large-scale processes, facilitating its broader use.