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-protein Interfaces02:04

Protein-protein Interfaces

15.0K
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...
15.0K

You might also read

Related Articles

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

Sort by
Same author

UTag, a cysteine-free thermostable tagging system for tracking single mRNA translation live.

Research square·2026
Same author

UTag, a cysteine-free thermostable tagging system for tracking single mRNA translation live.

bioRxiv : the preprint server for biology·2026
Same author

Efficiency Enhancement and Transparency Adaption of Bladed PM6:Y6 Solar Cells Doped with Binary Lanthanide (Eu<sup>3+</sup>/Sm<sup>3+</sup>)-Induced Polymeric Nanoaggregates.

ACS applied materials & interfaces·2026
Same author

Eu<sup>3+</sup> Complex-Protein Co-Crystals as Smart Sensors of Biologically Relevant Cations in Blood.

Materials (Basel, Switzerland)·2026
Same author

Modular Scaffold Crystals for Programmable Installation and Structural Observation of DNA-Binding Proteins.

bioRxiv : the preprint server for biology·2026
Same author

AI-assisted protein design to rapidly convert antibody sequences to intrabodies targeting diverse peptides and histone modifications.

Science advances·2026
Same journal

Nanotechnology-Stem Cell Strategies in 3D Glioblastoma Organoid: Targeting Glioma Stem Cells Within a Complex Tumor Microenvironment.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Mapping the 3D Chromosome Organization of a Biosynthetic Gene Cluster by Capture Hi-C (CHi-C).

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Mapping the 3D Chromosome Organization of Streptomyces by Hi-C.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

CUT&Tag Epigenomic Profiling of Biosynthetic Gene Clusters in Arabidopsis thaliana.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Rhizobium rhizogenes-Mediated Hairy Root Transformation Protocol for Lotus japonicus and Other Legumes.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Characterization of Bioactive Saponins from Sea Cucumbers.

Methods in molecular biology (Clifton, N.J.)·2026
See all related articles

Related Experiment Video

Updated: Mar 22, 2026

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

17.7K

A Structure-Based Design Protocol for Optimizing Combinatorial Protein Libraries.

Mark W Lunt1, Christopher D Snow2

  • 1Department of Chemical and Biological Engineering, Colorado State University, Fort Collins, CO, 80523, USA.

Methods in Molecular Biology (Clifton, N.J.)
|April 21, 2016
PubMed
Summary
This summary is machine-generated.

This study introduces a smarter method for creating protein variant libraries using combinatorial optimization, moving beyond traditional saturation mutagenesis. This approach designs libraries enriched for favorable, low-energy protein sequences, improving protein engineering efficiency.

Keywords:
Cluster expansionDegenerate codon optimizationProtein library designRational mutagenesisRegressionSaturation mutagenesis

More Related Videos

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

8.3K
Efficient Sampling of Genetically Encoded Biosensor Design Space Enabled with a Design of Experiments and Automation Workflow
08:58

Efficient Sampling of Genetically Encoded Biosensor Design Space Enabled with a Design of Experiments and Automation Workflow

Published on: October 17, 2025

793

Related Experiment Videos

Last Updated: Mar 22, 2026

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

17.7K
Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

8.3K
Efficient Sampling of Genetically Encoded Biosensor Design Space Enabled with a Design of Experiments and Automation Workflow
08:58

Efficient Sampling of Genetically Encoded Biosensor Design Space Enabled with a Design of Experiments and Automation Workflow

Published on: October 17, 2025

793

Area of Science:

  • Protein engineering
  • Molecular biology
  • Biotechnology

Background:

  • Site-directed mutagenesis is key for engineering proteins with altered functions, like enzyme specificity.
  • Conventional methods use saturation mutagenesis, encoding all 20 amino acids, which can be inefficient.

Purpose of the Study:

  • To present a protocol for designing "smarter" degenerate codon libraries.
  • To demonstrate enrichment of favorable, low-energy protein sequences using combinatorial optimization.

Main Methods:

  • Direct combinatorial optimization within "library space" to design degenerate codon libraries.
  • Utilizing a standard all-atom scoring function to assess sequence energy.
  • Applying Pareto analysis for library size and cost optimization.

Main Results:

  • Case studies show successful design of degenerate codon libraries highly enriched for favorable sequences.
  • The proposed method offers an alternative to traditional site saturation mutagenesis.
  • Enrichment of low-energy sequences was confirmed via computational assessment.

Conclusions:

  • Designing degenerate codon libraries via combinatorial optimization is a powerful strategy for protein engineering.
  • This "smarter" approach enhances efficiency and focuses on desirable protein variants.
  • Experimental labs can benefit by adopting these advanced library design principles.