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Related Concept Videos

Peptide Bonds02:43

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...
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.
Translocation of Proteins into the Mitochondria01:19

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,...
Protein Folding01:25

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 Folding01:22

Protein Folding

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Related Experiment Video

Updated: Jun 30, 2026

Determination of the Gas-phase Acidities of Oligopeptides
11:00

Determination of the Gas-phase Acidities of Oligopeptides

Published on: June 24, 2013

Electron transfer in peptides and proteins.

Bernd Giese1, Michael Graber, Meike Cordes

  • 1Department of Chemistry, University of Basel, St. Johanns Ring 19, CH-4056 Basel, Switzerland. bernd.giese@unibas.ch

Current Opinion in Chemical Biology
|September 23, 2008
PubMed
Summary

Proteins facilitate electron transfer through amino acids via single-step or multistep hopping. Multistep hopping allows fast, long-distance electron transfer, crucial for biological processes like those in enzymes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Proteins and peptides mediate electron transfer reactions using amino acids.
  • Electron transfer can occur via single-step superexchange or multistep hopping.
  • Hopping processes are less dependent on distance compared to single-step transfer.

Purpose of the Study:

  • To explain the mechanisms of electron transfer in proteins and peptides.
  • To highlight the role of amino acid side chains in facilitating electron hopping.
  • To emphasize the importance of multistep hopping for long-distance electron transfer in biological systems.

Main Methods:

  • Theoretical analysis of electron transfer mechanisms.
  • Review of experimental evidence for electron hopping in proteins.
  • Case study of electron transfer in ribonucleotide reductase.

Main Results:

  • Electron hopping, enabled by oxidizable amino acid side chains (e.g., tyrosine), acts as an intermediate charge carrier.
  • Multistep hopping processes exhibit weak distance dependency, allowing efficient electron transfer over long distances.
  • Enzymes like ribonucleotide reductase utilize this mechanism for rapid, long-range electron transfer.

Conclusions:

  • Multistep electron hopping is a key mechanism for efficient long-distance electron transfer in biological systems.
  • The distance-independent nature of hopping makes it vital for the function of complex enzymes.
  • Understanding these electron transfer pathways is crucial for deciphering protein function and designing novel biomimetic systems.