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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.0K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.2K
No description available
2.2K
Combinatorial Gene Control02:33

Combinatorial Gene Control

9.7K
Combinatorial gene control is the synergistic action of several transcriptional factors to regulate the expression of a single gene. The absence of one or more of these factors may lead to a significant difference in the level of gene expression or repression.
The expression of more than 30,000 genes is controlled by approximately 2000-3000 transcription factors. This is possible because a single transcription factor can recognize more than one regulatory sequence. The specificity in gene...
9.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.8K
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...
14.8K
Protein Networks02:26

Protein Networks

4.6K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.6K
Protein Complex Assembly02:41

Protein Complex Assembly

16.9K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.9K

You might also read

Related Articles

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

Sort by
Same author

Terminal-Directed Supramolecular Liquid Crystal Formation by Designed Coiled-Coil Interparticle Stacking.

ACS nano·2026
Same author

Patchy peptide particles for pH-responsive assembly into liquid crystals or lattices.

Science (New York, N.Y.)·2026
Same author

Electrostatic Coassembly of Coiled-Coil Peptide Bundlemers with Complementary Charges into Porous 2D Lattices.

Journal of the American Chemical Society·2025
Same author

Protein-Based Nanostructures: Column-free Biosynthesis of Bundlemer Peptides with Programmable, Orthogonally Reactive Handles for Nanomaterial Construction.

ACS applied materials & interfaces·2025
Same author

Designed coiled-coil peptide nanoparticles with tunable self-assembly: distinct ordered nanostructures <i>via</i> nonnatural side chain modification and electrostatic screening.

Soft matter·2025
Same author

Super-expansive thermo-reversible interstitial solid solution of nanocrystal superlattices with mesogens.

Nature materials·2025
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

Related Experiment Video

Updated: Feb 22, 2026

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

1.2K

Combinatorial protein design.

Jeffery G Saven1

  • 1Department of Chemistry, University of Pennsylvania, 231 South 34 Street, Philadelphia 19104, USA. saven@sas.upenn.edu

Current Opinion in Structural Biology
|August 7, 2002
PubMed
Summary
This summary is machine-generated.

Combinatorial protein libraries enable exploring many sequences for protein design and folding studies. New theoretical tools help manage sequence diversity in these libraries for better experiments.

More Related Videos

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.8K
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

Related Experiment Videos

Last Updated: Feb 22, 2026

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

1.2K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.8K
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

Area of Science:

  • Protein engineering and computational biology.
  • Structural biology and biophysics.

Background:

  • Combinatorial protein libraries allow for the investigation of diverse amino acid sequences.
  • These libraries are crucial for de novo protein design and understanding protein folding mechanisms.
  • The vast number of potential protein sequences presents a challenge for library diversity.

Purpose of the Study:

  • To introduce theoretical tools for biasing and characterizing sequence ensembles in combinatorial libraries.
  • To enhance the design and interpretation of experiments using protein sequence diversity.

Main Methods:

  • Development of theoretical frameworks to guide sequence selection in combinatorial libraries.
  • Methods for characterizing the ensemble of sequences predicted to fold into a specific structure.

Main Results:

  • Theoretical tools have been advanced to manage and analyze the diversity of sequences within combinatorial libraries.
  • These tools facilitate the creation of libraries biased towards desired structural or functional properties.

Conclusions:

  • Theoretical advancements enable more effective use of combinatorial protein libraries.
  • These tools are vital for the rational design of proteins and for deciphering folding principles.