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 Organization01:13

Protein Organization

152.5K
Overview
152.5K
Protein Organization01:24

Protein Organization

8.3K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
8.3K
Protein Folding01:22

Protein Folding

124.5K
Overview
124.5K
Protein Folding01:25

Protein Folding

10.0K
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...
10.0K
Protein and Protein Structure02:15

Protein and Protein Structure

84.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
84.5K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

13.6K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.6K

You might also read

Related Articles

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

Sort by
Same author

Topology-Aware Generation and Activity-Based Filtering: A Computational-Experimental Framework for Data-Scarce Quaternary Ammonium Compound Discovery.

Journal of chemical information and modeling·2026
Same author

DyVarMap: Integrating Conformational Dynamics and Interpretable Machine Learning for Cancer-Associated Missense Variant Classification in FGFR2.

Bioengineering (Basel, Switzerland)·2026
Same author

Predicting epistasis across proteins by structural logic.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Efficient High-Throughput DNA Breathing Features Generation Using Jax-EPBD.

bioRxiv : the preprint server for biology·2024
Same author

DNA breathing integration with deep learning foundational model advances genome-wide binding prediction of human transcription factors.

Nucleic acids research·2024
Same author

Elucidating the Role of Wildtype and Variant FGFR2 Structural Dynamics in (Dys)Function and Disorder.

International journal of molecular sciences·2024

Related Experiment Video

Updated: Nov 15, 2025

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.3K

Generative Adversarial Learning of Protein Tertiary Structures.

Taseef Rahman1, Yuanqi Du1, Liang Zhao2

  • 1Department of Computer Science, George Mason University, Fairfax, VA 22030, USA.

Molecules (Basel, Switzerland)
|March 6, 2021
PubMed
Summary
This summary is machine-generated.

Generative adversarial networks (GANs) can model protein structures, but Wasserstein GAN effectively captures complex patterns. This deep learning approach aids in exploring diverse protein structures for cellular functions.

Keywords:
deep learninggenerative adversarial learningprotein modelingtertiary structure

More Related Videos

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

611
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

17.3K

Related Experiment Videos

Last Updated: Nov 15, 2025

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.3K
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

611
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

17.3K

Area of Science:

  • Computational Biology
  • Structural Biology
  • Deep Learning

Background:

  • Protein molecules exhibit dynamic tertiary structures crucial for molecular interactions.
  • Accurately predicting these structures under physiological conditions is a significant challenge.

Purpose of the Study:

  • To investigate the efficacy of generative adversarial networks (GANs) in generating physically realistic protein tertiary structures.
  • To identify effective GAN models and training strategies for capturing complex protein structural patterns.

Main Methods:

  • Evaluation of several GAN models for their ability to generate protein tertiary structures.
  • Analysis of training stabilization mechanisms and their impact on GAN performance.
  • Comparative assessment of Wasserstein GAN against other models for structural pattern fidelity.

Main Results:

  • Many GAN models struggle to capture intricate, long-range structural patterns in proteins.
  • Not all proposed GAN training stabilization techniques are universally effective.
  • GAN performance metrics like loss may not correlate with the quality of generated structural datasets.
  • Wasserstein GAN demonstrates a superior ability to capture both local and distal structural features.

Conclusions:

  • Wasserstein GAN represents a promising advancement in deep generative models for protein structure prediction.
  • This approach offers a pathway to explore the diverse structural landscape of proteins and their functions.
  • Further development of GANs can enhance our understanding of protein dynamics and cellular activities.