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Peptide Bonds

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

Preparation and Reactions of Sulfides

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 RER

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.

Preparation and Reactions of Thiols

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.

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Protein Folding

Protein Folding

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Related Experiment Video

Updated: Jul 5, 2026

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

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

Published on: October 2, 2018

Disulfide bond formation in peptides.

Lin Chen¹, Ioana Annis², George Barany³

¹AxCell Biosciences Corporation, Newtown, Pennsylvania.

Current Protocols in Protein Science

|April 23, 2008

Summary

This summary is machine-generated.

This study details methods for creating disulfide bridges, essential for peptide folding and stability. These techniques enhance peptide structure, specificity, and biological activity in complex molecules.

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Area of Science:

Biochemistry
Peptide Chemistry
Structural Biology

Background:

Disulfide bridges are critical for the folding, structural stabilization, and biological activity of natural peptides and proteins.
Artificial introduction of disulfide bridges can enhance specificity and stability of natural or designed peptides.

Purpose of the Study:

To provide a selection of state-of-the-art procedures for forming disulfide bridges.
To enable the establishment of intramolecular or intermolecular disulfide bridges in peptides of varying complexity.

Main Methods:

Selective procedures for disulfide bond formation.
Techniques applicable to diverse peptide targets.

Main Results:

Successful establishment of disulfide bridges in complex peptide targets.
Demonstration of a selective menu of disulfide-forming procedures.

Conclusions:

The presented methods offer a valuable toolkit for peptide chemists and structural biologists.
Disulfide bridge formation is a key strategy for optimizing peptide function and stability.