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Related Concept Videos

Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

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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.
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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.
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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.
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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,...
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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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DiPTH-Cystine and PTH-Cysteine in Disulfide Bond Analysis Using Automated Edman Degradation.

Toni Kühl1, Yomnah Y Elsayed2, Alexander Terekhov1

  • 1Pharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn, Bonn, Germany.

Journal of Peptide Science : an Official Publication of the European Peptide Society
|August 29, 2025
PubMed
Summary

This study enhances disulfide bridge analysis in peptides using Edman sequencing. By comparing PTH-derivatives, researchers accurately identify cysteine connectivity, simplifying structural elucidation for cysteine-rich proteins.

Keywords:
Edman degradationconotoxincysteinedisulfide bridgesinsulinpeptides

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Analytical Chemistry

Background:

  • Disulfide bridges are crucial for protein structure and function.
  • Accurate annotation of disulfide bonds is challenging, requiring extensive data analysis.
  • Current methods for disulfide bond assignment can be complex and prone to errors.

Purpose of the Study:

  • To improve the elucidation of cysteine connectivity in peptides and proteins.
  • To provide a reliable method for disulfide bond assignment using Edman sequencing.
  • To facilitate structural analysis of cysteine-rich molecules.

Main Methods:

  • Re-implementation of Edman sequencing for disulfide bridge analysis.
  • Synthesis of diPTH-cystine and PTH-cysteine standards for comparison.
  • Application of automated Edman sequencing to peptides with multiple disulfide bonds.

Main Results:

  • Successful identification of disulfide bonds by detecting specific PTH-derivatives during Edman sequencing.
  • Differentiation of half-cystines involved in disulfide bridges, even within the same or separate sequencing cycles.
  • Demonstrated utility in analyzing peptides with two or three disulfide bridges.

Conclusions:

  • Edman sequencing, with synthesized standards, offers a robust approach to disulfide bond assignment.
  • This method simplifies the structural elucidation of complex cysteine-rich peptides and proteins.
  • The combined approach aids in accurate annotation of disulfide bridges, reducing structural analysis errors.