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

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

You might also read

Related Articles

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

Sort by
Same author

Lycopene pathway rewiring by combinatorial co-expression of constituent enzymes in a cell-free protein synthesis system.

New biotechnology·2026
Same author

Interaction Persistence-Based Identification of Key Binding Residues in the Cellular Retinol-Binding Protein 1 Complex.

Journal of chemical information and modeling·2026
Same author

Synergistic Potential of Repurposing non-β-lactam Compounds as Class A serine β-lactamases Inhibitor: Insights from MolecularDocking, Molecular Dynamics Simulations and Antimicrobial Potentiation.

Scientific reports·2026
Same author

Quantitative characterization of molecular motions using Rigid Body Transformation in molecular dynamics simulations.

Journal of biomolecular structure & dynamics·2026
Same author

Directed evolution-driven reprogramming of PD-L1 for compact and tunable checkpoint modulation.

Journal of biological engineering·2025
Same author

Corrigendum to "Integrated cascade biocatalysis of cannabigerolic acid through cyclodextrin-mediated stabilization and prenyltransferase engineering". [Bioresour. Technol. 438 (2025) 133190].

Bioresource technology·2025
Same journal

Epidemiological characteristics of amebiasis in Japan from 2001 to 2022.

PloS one·2026
Same journal

Longitudinal associations of academic stress with eating related patterns, nutrition, somatic indicators, and depressive symptoms in university students: A study protocol.

PloS one·2026
Same journal

Pollution removal efficiency enhancement by agricultural biomass additions in constructed wetlands: A framework integrating meta-analysis with explainable machine learning.

PloS one·2026
Same journal

Insulation failure mapping on power transformer bushing using FRA and electrostatic simulation.

PloS one·2026
Same journal

Enhancing medical Q&A systems with multimodal knowledge graphs and dual-layer attention mechanisms.

PloS one·2026
Same journal

UAMP: Consistent video object segmentation with uncertainty-aware memory propagation.

PloS one·2026
See all related articles

Related Experiment Video

Updated: May 16, 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

Deletional protein engineering based on stable fold.

Govindan Raghunathan1, Nagasundarapandian Soundrarajan, Sriram Sokalingam

  • 1Department of Chemical Engineering, Pusan National University, Busan, South Korea.

Plos One
|December 15, 2012
PubMed
Summary
This summary is machine-generated.

Deletion mutagenesis in protein engineering is enhanced by using highly stable proteins, like stable green fluorescent protein (s-GFP). This approach overcomes structural disruptions, enabling exploration of new protein variants.

More Related Videos

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Related Experiment Videos

Last Updated: May 16, 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

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Area of Science:

  • Protein engineering
  • Structural biology
  • Biophysics

Background:

  • Diversifying protein sequence-structure space is crucial for protein engineering.
  • Deletion mutagenesis offers unique sequence-structure exploration but often causes detrimental structural perturbations and protein inactivation.
  • Substitution mutagenesis is more common due to fewer structural disruptions.

Purpose of the Study:

  • To investigate if high protein stability can mitigate the drawbacks of deletion mutagenesis in protein engineering.
  • To explore the potential of deletion mutagenesis in generating novel protein variants using a stable green fluorescent protein (s-GFP) model system.

Main Methods:

  • Systematic deletion mutagenesis of N-terminal, C-terminal, and internal sequences of both normal stability GFP (n-GFP) and stable GFP (s-GFP).
  • Characterization of generated variants (s-DL4, s-N14, s-C225) for activity and biophysical properties.
  • Computational modeling for structural analysis of variants and their spectral properties.

Main Results:

  • Highly stable s-GFP demonstrated greater tolerance to amino acid deletions compared to n-GFP.
  • Novel variants (s-DL4, s-N14, s-C225) were successfully generated from s-GFP through deletion mutagenesis, which were unobtainable from n-GFP.
  • Variant s-DL4, with loop deletions, showed predominantly insoluble but active forms. Variants s-N14 and s-C225, lacking residues involved in secondary structures, exhibited comparable biophysical properties to n-GFP.
  • Computational modeling provided structural insights into the spectral properties of the variants.

Conclusions:

  • Employing highly stable protein structures can overcome the limitations of deletion mutagenesis in protein engineering.
  • This strategy significantly enhances the exploration of protein sequence-structure space for deletion mutants.
  • High-stability proteins are promising platforms for generating diverse and potentially functional protein variants via deletion mutagenesis.