Jove
Visualize
Contact Us
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 Concept Videos

From DNA to Protein03:06

From DNA to Protein

24.8K
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...
24.8K
RNA Stability01:53

RNA Stability

36.4K
Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
36.4K
RNA Stability01:53

RNA Stability

12.2K
12.2K
Leaky Scanning02:28

Leaky Scanning

5.9K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.9K
Nonsense-mediated mRNA Decay02:27

Nonsense-mediated mRNA Decay

12.2K
The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
Usually, Upf3 binds to an Exon Junction Complex (EJC) at mRNA splice sites. If a ribosome fully translates the mRNA,...
12.2K
Improving Translational Accuracy02:07

Improving Translational Accuracy

15.6K
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...
15.6K

You might also read

Related Articles

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

Sort by
Same author

Endocrine dysfunction induced by anti-PD-1 antibody and tyrosine kinase inhibitor in a pediatric patient with renal cell carcinoma.

Clinical pediatric endocrinology : case reports and clinical investigations : official journal of the Japanese Society for Pediatric Endocrinology·2026
Same author

Nationwide trends in outcomes and resource utilization in surgically treated acute type A aortic dissection with coronary malperfusion.

JTCVS open·2026
Same author

Systematic Exploration of Synthesis and Function Landscapes for DNA Hydrogels.

ACS synthetic biology·2026
Same author

Haemodynamic Early Outcomes of Sinus Plication for Bicuspid Aortic Valve Repair.

Interdisciplinary cardiovascular and thoracic surgery·2026
Same author

The association of extracellular vesicle (EV)-cargo miR-330-3p with postoperative delirium and a potential mechanism of tau phosphorylation and neuron toxicity.

bioRxiv : the preprint server for biology·2026
Same author

Hidden diversity of marine zooplankton under sea ice in the Okhotsk Sea: Insights from community and population analyses based on DNA metabarcoding.

Marine environmental research·2026

Related Experiment Video

Updated: Apr 12, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.6K

Protein stabilization utilizing a redefined codon.

Kazumasa Ohtake1, Atsushi Yamaguchi1, Takahito Mukai1

  • 11] Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan [2] RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.

Scientific Reports
|May 19, 2015
PubMed
Summary

Protein structural stability can be enhanced by incorporating bulky halogenated amino acids. This bioengineering approach significantly stabilizes proteins like glutathione S-transferase and azoreductase.

More Related Videos

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers
10:41

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers

Published on: June 24, 2019

8.9K
Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
11:47

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Published on: August 1, 2016

16.5K

Related Experiment Videos

Last Updated: Apr 12, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.6K
Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers
10:41

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers

Published on: June 24, 2019

8.9K
Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
11:47

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Published on: August 1, 2016

16.5K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioengineering

Background:

  • Synthetic amino acid incorporation into proteins has advanced significantly.
  • This allows for efficient, multiple-site incorporation beyond the 20 canonical amino acids.
  • These advancements offer new strategies for bioengineering challenges.

Purpose of the Study:

  • To investigate if integrating bulky halogenated amino acids can enhance protein structural stability.
  • To explore a novel mechanism for protein stabilization using non-canonical amino acids.

Main Methods:

  • Incorporation of 3-chloro- and 3-bromo-l-tyrosines into glutathione S-transferase at seven selected sites.
  • Assessment of protein stabilization using techniques such as glutathione S-transferase.
  • X-ray crystallographic analysis to elucidate the structural basis of stabilization.
  • Application of the method to stabilize the industrially relevant azoreductase.

Main Results:

  • Glutathione S-transferase was significantly stabilized by 5.2 and 5.6 kcal/mol with the incorporated halogenated tyrosines.
  • X-ray crystallography revealed that bulky halogen moieties filled internal protein spaces.
  • Non-canonical stabilizing interactions between halogen moieties and neighboring residues were observed.
  • Rapid stabilization of azoreductase demonstrated the broad applicability of the method.

Conclusions:

  • Integrating bulky halogenated amino acids is an effective strategy for enhancing protein structural stability.
  • This method provides a simple and broadly applicable mechanism for protein stabilization in bioengineering.
  • The findings open new avenues for designing more robust and functional proteins for industrial applications.