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

tRNA Activation

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...

You might also read

Related Articles

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

Sort by

Same author

Combination of single-molecule Förster resonance energy transfer and hydrogen-deuterium exchange mass spectrometry toward dynamic structural biology.

Current opinion in structural biology·2026

Same author

An allosteric network governs Tom70 conformational dynamics to coordinate mitochondrial import.

Structure (London, England : 1993)·2025

Same author

Synthetic Type III-E CRISPR-Cas Effectors for Programmable RNA-targeting.

Journal of molecular biology·2025

Same author

The Mechanism of Histone Ubiquitylation by the ASB9-CUL5 Ubiquitin Ligase.

Molecular & cellular proteomics : MCP·2025

Same author

A Structurally Divergent Class Ia Ribonucleotide Reductase from a Tick-Borne Pathogen.

Biochemistry·2025

Same author

An allosteric network governs Tom70 conformational dynamics to coordinate mitochondrial protein import.

bioRxiv : the preprint server for biology·2025

Search research articles

Related Experiment Video

Updated: Apr 25, 2026

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

Trypsinogen activation as observed in accelerated molecular dynamics simulations.

Leonardo Boechi¹, Levi Pierce, Elizabeth A Komives

¹Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, California.

Protein Science : a Publication of the Protein Society

|August 19, 2014

Summary

Accelerated molecular dynamics simulations revealed the N-terminal tail insertion mechanism in serine proteases. This study highlights the hydrophobic effect

Keywords:

GIST MD aMD accelerated molecular dynamics molecular dynamics solvation trypsin trypsinogen

More Related Videos

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

Published on: September 26, 2020

Related Experiment Videos

Last Updated: Apr 25, 2026

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

Published on: September 26, 2020

Area of Science:

Biochemistry
Molecular Biology
Computational Chemistry

Background:

Serine proteases regulate vital physiological processes.
Enzyme activity is controlled by activation from an inactive zymogen form via cleavage.
Early molecular dynamics simulations of trypsin were limited by computational power.

Purpose of the Study:

To elucidate the N-terminal tail insertion mechanism during serine protease activation.
To investigate the forces driving the zymogen to active enzyme transition.
To provide new thermodynamic insights into serine protease activation.

Main Methods:

Utilized accelerated molecular dynamics (aMD) simulations.
Enhanced configurational sampling for atomistic simulations.
Focused on the activation mechanism of trypsin, a key serine protease.

Main Results:

Successfully observed the N-terminal tail insertion, a critical activation step.
Provided evidence that hydrophobic effects are the primary drivers of tail insertion.
Identified significant enthalpic contributions to the overall activation process.

Conclusions:

The N-terminal tail insertion is a conserved mechanism in serine protease activation.
Hydrophobic effects play a crucial role in guiding this insertion.
The findings offer novel perspectives on the thermodynamics of serine protease activation.