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

Protein-Drug Binding: Determination Methods

Protein-Drug Binding: Determination Methods

Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...

Protein Digestion

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

Mechanical Protein Functions

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.

You might also read

Related Articles

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

Sort by

Same author

Inhibition of soluble epoxide hydrolase ameliorates renal injury in IgA nephropathy by restoring epoxyeicosatrienoic acids.

iScience·2026

Same author

Noni (<i>Morinda citrifolia</i> L.) fruit juice induces ferroptosis in gastric cancer cells <i>via</i> the Nrf2/HO-1-GPX4 axis.

Food & function·2026

Same author

From modular engineering to practical applications: Advances in GPCR-based yeast biosensors.

Biotechnology advances·2026

Same author

Targeting CDC42 Protects Mitochondrial Function through KLF2/HIF-1α/PINK1 Signaling in Acute Kidney Injury.

International journal of biological sciences·2026

Same author

Feature-Based Statistical Learning Modulates Distractor Interference, Not Distractor Rarity.

Psychophysiology·2025

Same author

High-Sucrose Diet-Induced Reprogramming of Plasma Oxylipin Profiles Reflects Dietary Risk for Gut Barrier Dysfunction.

Journal of agricultural and food chemistry·2025

Search research articles

Related Experiment Video

Updated: Feb 12, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

A Facile Method for Producing Selenocysteine-Containing Proteins.

Takahito Mukai¹, Anastasia Sevostyanova¹, Tateki Suzuki¹

¹Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.

Angewandte Chemie (International Ed. in English)

|April 10, 2018

Summary

This summary is machine-generated.

Researchers developed a new method to insert multiple selenocysteine (Sec) residues into proteins using engineered Escherichia coli. This allo-tRNA system enables precise selenoprotein synthesis for novel protein functions.

Keywords:

genetic code expansion protein engineering selenocysteine selenoproteins synthetic biology

More Related Videos

Design and Construction of an Urban Runoff Research Facility

Design and Construction of an Urban Runoff Research Facility

Published on: August 8, 2014

Author Spotlight: Optimizing Apoplast Protein Extraction for Efficient Recovery of Recombinant Proteins from Plant Cells

Author Spotlight: Optimizing Apoplast Protein Extraction for Efficient Recovery of Recombinant Proteins from Plant Cells

Published on: July 5, 2024

Related Experiment Videos

Last Updated: Feb 12, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Design and Construction of an Urban Runoff Research Facility

Design and Construction of an Urban Runoff Research Facility

Published on: August 8, 2014

Author Spotlight: Optimizing Apoplast Protein Extraction for Efficient Recovery of Recombinant Proteins from Plant Cells

Author Spotlight: Optimizing Apoplast Protein Extraction for Efficient Recovery of Recombinant Proteins from Plant Cells

Published on: July 5, 2024

Area of Science:

Biochemistry
Molecular Biology
Synthetic Biology

Background:

Selenocysteine (Sec) incorporation into proteins imparts unique chemical properties.
Existing methods for site-specific Sec insertion are limited.
Expanding the genetic code is crucial for novel protein engineering.

Purpose of the Study:

To develop a facile method for synthesizing selenoproteins with multiple Sec residues.
To engineer Escherichia coli for enhanced selenoprotein production.
To create a versatile platform for selenoprotein engineering.

Main Methods:

Discovery and utilization of allo-tRNAs as efficient serine acceptors.
Conversion of serine-accepting allo-tRNAs to selenocysteine-accepting allo-tRNAs using Aeromonas salmonicida selenocysteine synthase (SelA).
Engineering of E. coli selenium metabolism and modification of allo-tRNA and SelA for improved yields.

Main Results:

Demonstrated successful read-through of five UAG codons in fdhF mRNA using Sec-allo-tRNA variants.
Produced active formate dehydrogenase H (FDH _H) with five Sec residues in E. coli.
Achieved over 80% yield and purity for recombinant human glutathione peroxidase 1 (GPx1) using the engineered system.

Conclusions:

The allo-tRNA ^UTu system provides a novel and efficient platform for selenoprotein engineering.
This method allows for the synthesis of selenoproteins with multiple Sec residues at desired positions.
The engineered E. coli system enhances the production of valuable selenoproteins.