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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.5K
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...
19.5K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.6K
14.6K
Protein Folding01:25

Protein Folding

10.9K
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...
10.9K
Protein Folding01:22

Protein Folding

125.7K
Overview
125.7K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.1K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.1K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.7K
2.7K

You might also read

Related Articles

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

Sort by
Same author

Multimerization interactions between protein-inspired single-chain random heteropolymers.

PloS one·2026
Same author

Conformational flexibility of talin enables force-free sampling of activation-competent states.

Communications chemistry·2026
Same author

Polymerized Short Sequences as a Template for Protein Folding and Evolution.

Nano letters·2026
Same author

Computational design of functional random heteropolymers through atomistic simulations.

PloS one·2026
Same author

Polyanion Chemistry Engineers Ternary RNA Nanoparticle Structure/Function from the Inside-Out.

ACS nano·2026
Same author

Computational design of conformation-biasing mutations to alter protein functions.

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

The x-ray absorption spectrum of the propargyl radical C3H3●.

The Journal of chemical physics·2026
Same journal

Transient hydroperoxyalkyl intermediates (•QOOH) in isopentane oxidation. I. Conformer- and isomer-resolved infrared spectra.

The Journal of chemical physics·2026
Same journal

Transient hydroperoxyalkyl intermediates (•QOOH) in isopentane oxidation. II. Isomer-resolved unimolecular dynamics.

The Journal of chemical physics·2026
Same journal

Quantum state-to-state dynamics studies of the C(3P) + OH(X2Π) → CO(a3Π) + H(2S) reaction based on a new HCO(12A″) potential energy surface.

The Journal of chemical physics·2026
Same journal

Time-resolved ultrabroadband far-to-mid-infrared spectroscopy directly reveals doorway-mediated vibrational energy flow in an energetic crystal (β-HMX).

The Journal of chemical physics·2026
Same journal

Anomalous phase behaviors near the multiphase coexistence point in 1-alkyl-3-methylimidazolium ionic liquids.

The Journal of chemical physics·2026
See all related articles
  1. Home
  2. Repetitive Proteins That Undergo Large Conformational Changes Evade Structural Prediction Algorithms.
  1. Home
  2. Repetitive Proteins That Undergo Large Conformational Changes Evade Structural Prediction Algorithms.

Related Experiment Video

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

7.6K

Repetitive proteins that undergo large conformational changes evade structural prediction algorithms.

Marina P Chang1, Tianyi Jin2,3, Alana P Gudinas4

  • 1Department of Materials Science and Engineering, Stanford University, Stanford, California 94305, USA.

The Journal of Chemical Physics
|December 11, 2025

View abstract on PubMed

Summary
This summary is machine-generated.

Protein structure prediction tools like AlphaFold struggle with dynamic proteins. New RTX protein variants show diverse structures, highlighting the need for better predictive models validated by experiments.

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

884
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

17.5K

Related Experiment 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

7.6K
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

884
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

17.5K

Area of Science:

  • Structural biology
  • Computational biology
  • Biochemistry

Background:

  • Protein structure prediction algorithms like AlphaFold have advanced protein design.
  • These tools face limitations with conformationally dynamic, intrinsically disordered, and stimuli-responsive proteins.

Purpose of the Study:

  • To evaluate sequence-to-structure predictions for challenging intrinsically disordered proteins.
  • To explore the structural behavior of repeats-in-toxin (RTX) protein variants.

Main Methods:

  • Designed RTX sequence variants with modified repeats.
  • Utilized AlphaFold2 and AlphaFold3 for initial structure prediction.
  • Employed molecular dynamics simulations, circular dichroism spectroscopy, small-angle X-ray scattering, and X-ray crystallography for experimental validation.

Main Results:

  • AlphaFold predicted β-roll structures for all RTX variants.
  • Experimental methods revealed diverse, sequence-dependent structures for RTX variants in different calcium conditions.
  • Predicted structures did not fully capture the experimental conformational dynamics.

Conclusions:

  • Current protein structure prediction tools need improvement for intrinsically disordered proteins.
  • Multi-modal, multi-scale experimental validation is crucial for accurate protein design.
  • Understanding sequence-structure relationships in dynamic proteins is key for biotechnology and sustainability.