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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...
Post-translational Translocation of Proteins to the RER01:27

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...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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,...
ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...

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Related Experiment Video

Updated: Jun 24, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Electron relay race in peptides.

Bernd Giese1, Min Wang, Jian Gao

  • 1Universität Basel, St. Johanns-Ring 19, 4056 Basel, Switzerland. bernd.giese@unibas.ch

The Journal of Organic Chemistry
|April 7, 2009
PubMed
Summary

A new peptide assay measures electron-transfer (ET) efficiencies. Two-step ET processes are faster than single-step reactions, utilizing specific amino acids as relays.

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Related Experiment Videos

Last Updated: Jun 24, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Molecular Biophysics

Background:

  • Electron transfer (ET) is fundamental in biological processes.
  • Understanding ET mechanisms in peptides is crucial for designing functional biomolecules.
  • Current methods for measuring peptide ET efficiencies are limited.

Purpose of the Study:

  • To develop a novel assay for quantifying electron-transfer efficiencies in peptides.
  • To investigate the kinetics of single-step versus multi-step ET reactions within peptide systems.
  • To identify amino acid residues that can effectively mediate charge transport.

Main Methods:

  • Development of a peptide-based assay for direct measurement of ET efficiencies.
  • Utilizing peptides with strategically placed aromatic and sulfur-containing amino acids.
  • Analysis of reaction kinetics to differentiate between single-step and two-step ET processes.

Main Results:

  • The developed assay successfully measures peptide ET efficiencies.
  • Two-step electron transfer processes were found to be kinetically faster than single-step pathways.
  • Aromatic and sulfur-containing aliphatic amino acids (e.g., tryptophan, histidine, cysteine) act as effective charge relays.
  • Proton-coupled electron transfer (PCET) was observed with specific amino acid combinations.

Conclusions:

  • The novel peptide assay provides a valuable tool for studying ET mechanisms.
  • Multi-step ET pathways offer a kinetic advantage, facilitated by specific amino acid residues.
  • The findings contribute to the understanding of charge transport in peptides and the role of specific amino acids, including PCET.