Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Initiation of Translation

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...

Initiation of Translation

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...

Termination of Translation

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...

Protein Organization

Protein Organization

Protein Organization

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.

Improving Translational Accuracy

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A general approach to unraveling structural changes of food proteins using atomistic model-based SAXS.

Food chemistry·2026

Same author

Deciphering high density lipoprotein (HDL) structure-function: Detailed analysis of HDL subfractions reveals molecular differences leading to atherosclerosis risk.

International journal of biological macromolecules·2026

Same author

Scattering from 'Babinet' particles (or not…): spherical particles made up of spheres and spherical particles with spherical voids.

Journal of applied crystallography·2026

Same author

The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2025

Same author

Antibiotic vesicles based on peptide-polymer complex coacervation.

Journal of colloid and interface science·2025

Same author

Divergent effects of anionic surfactants on laundry enzymes: Structural stability, activity modulation, and self-cleavage mechanisms.

International journal of biological macromolecules·2025

Search research articles

Related Experiment Video

Updated: May 27, 2026

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

Structure and dimerization of translation initiation factor aIF5B in solution.

Louise Carøe Vohlander Rasmussen¹, Cristiano Luis Pinto Oliveira, Olwyn Byron

¹Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10, DK-8000 Aarhus C, Denmark.

Biochemical and Biophysical Research Communications

|November 22, 2011

Summary

Archaeal translation initiation factor 5B (aIF5B) exists in both monomeric and dimeric forms in solution. Its structure in solution closely resembles its crystal structure, with glycerol inhibiting dimerization.

More Related Videos

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Published on: December 25, 2021

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Related Experiment Videos

Last Updated: May 27, 2026

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Published on: December 25, 2021

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Translation initiation factor 5B (IF5B) is crucial for initiating protein synthesis.
Understanding the solution structure of archaeal IF5B (aIF5B) is key to elucidating its function.
Previous studies indicated potential monomeric and dimeric forms of aIF5B.

Purpose of the Study:

To determine the solution structure of archaeal IF5B (aIF5B).
To investigate the monomer-dimer equilibrium of aIF5B in solution.
To compare the solution structure with the known crystal structure.

Main Methods:

Small-angle X-ray scattering (SAXS) and dynamic light scattering (DLS) were used to analyze aIF5B.
Sedimentation equilibrium (SE) and sedimentation velocity (SV) analytical ultracentrifugation (AUC) characterized the solution species.
Crystallographic structure was used to model and compute theoretical sedimentation coefficients.

Main Results:

aIF5B exists in both monomeric and dimeric forms in solution, with dimers being irreversible but comprising a small percentage (5.0-6.8%).
Sedimentation coefficients for monomer and dimer were determined as 3.64 S and 5.51 S, respectively, aligning with theoretical models.
SAXS data, particularly with glycerol to inhibit dimerization, confirmed a solution structure similar to the crystal structure, revealing an elongated conformation (Rg=37.5 Å, Dmax≈130 Å).

Conclusions:

The solution structure of aIF5B is highly consistent with its atomic resolution crystal structure.
Glycerol effectively inhibits aIF5B dimerization, allowing for the study of the monomeric form.
Structural differences exist between archaeal IF5B and its homolog, E. coli IF2.