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Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

Translocation of Proteins into the Mitochondria

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

Post-translational Translocation of Proteins to the RER

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

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...

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Related Experiment Video

Updated: Jun 23, 2026

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Electron transfer in peptides and proteins.

Meike Cordes¹, Bernd Giese

¹Department of Chemistry, University of Basel, St. Johanns Ring 19, CH-4056 Basel, Switzerland.

Chemical Society Reviews

|May 8, 2009

Summary

Electron transfer (ET) in proteins is key to cellular energy and metabolism. This review covers models of ET through peptides and proteins, explaining its biological significance.

Area of Science:

Biophysics
Biochemistry
Molecular Biology

Background:

Electron transfer (ET) processes are fundamental to cellular energy conversion and metabolic catalysis.
Understanding ET mechanisms in biological systems is crucial for deciphering cellular functions.

Purpose of the Study:

To provide a tutorial review on models explaining electron transfer through peptides and proteins.
To elucidate the biological relevance and significance of electron transfer in cellular processes.

Main Methods:

Discussion of theoretical and experimental models for ET in peptides and proteins.
Review of literature on biological systems where ET plays a critical role.

Main Results:

Comprehensive overview of established models describing ET pathways in biological macromolecules.

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Detailed explanation of how ET facilitates energy conversion and catalytic functions in cells.

Conclusions:

Electron transfer is a vital process in cellular bioenergetics and metabolism.
The models discussed provide a framework for understanding ET in biological contexts and its implications for health and disease.