Jove
Visualize
Contact Us

Related Concept Videos

From DNA to Protein03:06

From DNA to Protein

18.2K
The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
18.2K
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

6.6K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
6.6K
The Central Dogma01:25

The Central Dogma

124.8K
Overview
124.8K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.1K
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,...
3.1K
tRNA Activation02:26

tRNA Activation

19.2K
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...
19.2K

You might also read

Related Articles

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

Sort by
Same author

Binary solvent participation in crystals of a multi-aromatic 1,2,3-triazole.

Acta crystallographica. Section E, Crystallographic communications·2025
Same author

Color center creation by dipole stacking in crystals of 2-meth-oxy-5-nitro-aniline.

Acta crystallographica. Section E, Crystallographic communications·2024
See all related articles
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Video

Updated: Jun 19, 2025

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
10:43

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes

Published on: October 3, 2019

5.8K

A convenient five-segment cassette procedure for DNA insertions coding for novel peptides.

Jonathan Filley1

  • 1Oligometrics, Inc., Boulder, Colorado, United States of America.

Plos One
|July 26, 2024
PubMed
Summary

This study introduces a cost-effective DNA assembly method using short oligomers to create peptides up to 20 amino acids long. The technique enables rapid peptide design, synthesis, and analysis, with high sequence accuracy.

More Related Videos

Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

10.4K
Rapid, Enzymatic Methods for Amplification of Minimal, Linear Templates for Protein Prototyping using Cell-Free Systems
07:35

Rapid, Enzymatic Methods for Amplification of Minimal, Linear Templates for Protein Prototyping using Cell-Free Systems

Published on: June 14, 2021

2.7K

Related Experiment Videos

Last Updated: Jun 19, 2025

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
10:43

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes

Published on: October 3, 2019

5.8K
Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

10.4K
Rapid, Enzymatic Methods for Amplification of Minimal, Linear Templates for Protein Prototyping using Cell-Free Systems
07:35

Rapid, Enzymatic Methods for Amplification of Minimal, Linear Templates for Protein Prototyping using Cell-Free Systems

Published on: June 14, 2021

2.7K

Area of Science:

  • Molecular Biology
  • Synthetic Biology
  • Biochemistry

Background:

  • Efficient DNA assembly is crucial for peptide synthesis and protein engineering.
  • Current methods can be costly and time-consuming.
  • Developing rapid, economical DNA cassette assembly is needed for exploring peptide function.

Purpose of the Study:

  • To describe a novel DNA cassette assembly method using short, inexpensive oligomers.
  • To enable rapid design, synthesis, and analysis of peptides.
  • To facilitate the study of peptide properties like solubility and binding.

Main Methods:

  • Utilizing five-segment DNA cassettes with 20 nt overlaps.
  • Employing phosphate-free nicks for efficient insertion into plasmid DNA and transformation of E. coli.
  • Repairing nicks in vivo via an unknown mechanism.
  • Isolating peptides as C-terminal fusions with Green Fluorescent Protein (GFP).

Main Results:

  • Successful assembly of DNA cassettes coding for peptides up to 20 amino acids long.
  • High efficiency of insertion and transformation with up to three nicks.
  • Peptides are readily isolated as GFP fusions with approximately 1% error rate.
  • Demonstrated ability to mutate peptides to study residue effects on GFP-fusion solubility and IMAC retention.

Conclusions:

  • The described DNA assembly method is rapid, economical, and accurate.
  • It allows for efficient exploration of novel peptide sequences and their properties.
  • This technique accelerates research in synthetic biology, protein engineering, and drug discovery.