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Related Concept Videos

Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

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Updated: Jul 13, 2026

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
08:07

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

Mapping the electrostatic potential within the ribosomal exit tunnel.

Jianli Lu1, William R Kobertz, Carol Deutsch

  • 1Department of Physiology, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.

Journal of Molecular Biology
|July 17, 2007
PubMed
Summary

Electrostatic potentials within the ribosomal exit tunnel were measured for the first time. Introducing charged amino acids alters these potentials, impacting protein folding and function.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Structural Biology

Background:

  • Electrostatic potentials are crucial for molecular interactions, influencing protein folding, stability, and catalysis.
  • The ribosomal exit tunnel (RET) environment and its nascent peptide are subject to electrostatic forces.
  • Direct measurement of electrostatics within the RET has been lacking.

Purpose of the Study:

  • To map the electrostatic potential and accessibility along the ribosomal exit tunnel.
  • To investigate the impact of charged amino acids on the nascent peptide's electrostatic environment.
  • To understand the dielectric properties and electric field dynamics within the RET.

Main Methods:

  • Development of novel probes and experimental strategies.
  • Measurement of electrostatic potential distribution within the ribosomal exit tunnel.
  • Analysis of electrostatic consequences of incorporating charged amino acids into nascent peptides.

Main Results:

  • The electrostatic potential and accessibility were mapped across the entire length of the ribosomal exit tunnel.
  • The introduction of a charged amino acid into the nascent peptide was shown to alter the local electrostatic potential.
  • New insights into the tunnel's dielectric properties and the dynamics of its electric fields were obtained.

Conclusions:

  • Electrostatic potentials within the ribosomal exit tunnel can be measured using novel techniques.
  • Nascent peptide charge significantly influences the electrostatic environment inside the ribosomal exit tunnel.
  • These findings enhance our understanding of cotranslational folding and protein biogenesis within the ribosome.