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 Folding01:22

Protein Folding

Overview
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
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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 form...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Conservation of Protein Domains02:26

Conservation of Protein Domains

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 form...

You might also read

Related Articles

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

Sort by
Same author

Convergence is not correctness: context-dependent performance of enhanced-sampling methods across biological complexity.

Nature communications·2026
Same author

Compact Solvation Enables Sub-Minute Sodium-Ion Storage: A Data-Driven Perspective.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

A Holistic Eating Monitoring System Enabled by Textile Strain Sensors and Hierarchical Network.

IEEE transactions on bio-medical engineering·2026
Same author

Bushen Antai recipe attenuates recurrent spontaneous abortion by activating VEGFA/p-AKT/SESN2 to restore trophoblast endoplasmic reticulum homeostasis.

Journal of ethnopharmacology·2026
Same author

Depression and anxiety changes in patients after orthognathic surgery: a systematic review and meta-analysis.

The British journal of oral & maxillofacial surgery·2026
Same author

Biomimetic metamaterial-based interface for decoding heterogeneous mechanodermal activity.

Science advances·2026
Same journal

ORBIT-AMD: Ordinal Risk, Bilateral Imaging, and Trajectory Learning for Age-Related Macular Degeneration in Multi-Cohorts.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

Giant Topological Hall Effect Across a Broad Temperature Window in Co-Doped Mn<sub>3</sub>Sn Noncoplanar Antiferromagnets.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

A Pancreatitis-Inspired Trypsinogen Nanoplatform Reprograms Tumor-Associated Macrophages via NF-κB for Pancreatic Cancer Immunotherapy.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

Integrated Opto-Biomechatronics For Single Muscle Fibre Structure-Function Assessment: The MyoRobot 3.0.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

Radiation Resilient Synthetic Antiferromagnets-Based Neuromorphic Device for Sea Surface Temperature Reconstruction.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

Targeting WDR12 Unleashes T-Cell-Mediated Antitumor Activity in Melanoma by Destabilizing CD276.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
See all related articles
  1. Home
  2. Discriminator-guided Inverse Folding For Multi-property Protein Design.
  1. Home
  2. Discriminator-guided Inverse Folding For Multi-property Protein Design.

Related Experiment Video

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

Discriminator-Guided Inverse Folding for Multi-Property Protein Design.

Yuchuan Zheng1, Chuyi Liu2, Zhaoming Liu3,4

  • 1Institute for Advanced Study in Physics, Zhejiang University, Hangzhou, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|June 9, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

Discriminator-Guided Inverse Folding (DGIF) enables simultaneous multi-property optimization for de novo protein design. This framework overcomes data limitations, improving protein thermostability and solubility by guiding inverse folding models.

Keywords:
discriminator‐guided optimizationinverse folding modelmulti‐property optimizationstructure‐based protein design

More Related Videos

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

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

Related Experiment 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

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

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

Area of Science:

  • Protein engineering
  • Computational biology
  • Biochemistry

Background:

  • Designing proteins with multiple desired physicochemical properties is crucial for real-world applications.
  • Structure-based de novo protein design is a leading paradigm, but joint multi-property optimization remains a challenge.
  • Current methods struggle with multi-property optimization due to limited datasets with multiple property annotations.

Purpose of the Study:

  • To develop a novel framework for simultaneous multi-property optimization in de novo protein design.
  • To overcome the limitations of existing inverse folding methods that require multi-property annotated datasets.
  • To enable the design of proteins with improved and simultaneously optimized properties like thermostability and solubility.

Main Methods:

  • Introduced Discriminator-Guided Inverse Folding (DGIF), a framework guiding inverse folding models.
  • Utilized an auxiliary discriminator module integrating multiple single-property predictors.
  • Adjusted internal history states of the inverse folding model via the discriminator.

Main Results:

  • DGIF achieved substantial improvements in protein thermostability and solubility.
  • The framework successfully generated protein sequences optimized for multiple properties simultaneously.
  • Designed proteins demonstrated a significant shift towards the Pareto front, indicating optimal trade-offs.

Conclusions:

  • DGIF effectively enables multi-property optimization in structure-based protein design without multi-property datasets.
  • The developed framework significantly enhances key protein traits and facilitates joint optimization.
  • Experimental validation confirms DGIF's efficacy for designing proteins with tailored, multiple characteristics.