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Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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.

Sulfur Assimilation

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 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.

Structure and Nomenclature of Thiols and Sulfides

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...

Protein Folding

Protein Folding

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Related Experiment Video

Updated: Jun 7, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Trisulfides in proteins.

Rasmus Wedel Nielsen¹, Christine Tachibana, Niels Erik Hansen

¹Section for Biomolecular Sciences, Department of Biology, University of Copenhagen, Denmark.

Antioxidants & Redox Signaling

|October 28, 2010

Summary

This summary is machine-generated.

Trisulfides, a rare protein modification, are found in biological systems like garlic and may be more common than previously thought. This review explores their chemistry, detection, and roles in cellular metabolism.

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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

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Oligosulfides, including trisulfides, are prevalent in nature, with known beneficial properties in plants like garlic.
Protein trisulfides, involving an extra sulfur atom between cysteines, are an uncommon post-translational modification.
The prevalence of trisulfides in proteins may be underestimated due to increasing evidence of sulfide pools in tissues and their metabolic roles.

Purpose of the Study:

To review known proteins containing trisulfide bridges.
To provide an overview of trisulfide formation chemistry.
To summarize methods for detecting trisulfides in proteins.

Main Methods:

Literature review of scientific articles and databases.
Analysis of protein structures and modifications.
Examination of biochemical assays and analytical techniques for sulfur-containing modifications.

Main Results:

Identification of specific proteins confirmed to contain trisulfide bridges.
Detailed explanation of the chemical mechanisms underlying trisulfide bond formation.
Compilation of various analytical methods, including mass spectrometry and spectroscopic techniques, used for trisulfide detection.

Conclusions:

Trisulfide bridges represent a significant, yet potentially under-recognized, post-translational modification in proteins.
Understanding trisulfide chemistry and detection is crucial for exploring their biological functions.
Further research is warranted to fully elucidate the prevalence and roles of trisulfides in cellular processes and metabolism.