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

19.6K
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...
19.6K
Protein Folding01:22

Protein Folding

125.9K
Overview
125.9K
Protein Folding01:25

Protein Folding

11.0K
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...
11.0K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.0K
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...
14.0K
Conserved Binding Sites01:49

Conserved Binding Sites

5.0K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.0K

You might also read

Related Articles

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

Sort by
Same author

Repurposing salmon calcitonin for glioblastoma treatment: Targeting Yes-associated Protein (YAP)/ Transcriptional co‑activator with PDZ‑binding motif (TAZ) via hippo pathway activation.

Neuro-oncology advances·2026
Same author

ER stress-mediated impairment of hepatic lipid export is associated with steatosis in AKI-induced remote liver injury.

Scientific reports·2026
Same author

Interpreting Short-Term Safety in Robotic Bariatric Surgery: The Importance of What Drives the Outcome.

Journal of the American College of Surgeons·2026
Same author

Oxidative stress, antioxidant depletion, and DNA damage in post-COVID-19 patients: evidence of a disrupted redox network and loss of age-dependent antioxidant compensation.

Naunyn-Schmiedeberg's archives of pharmacology·2026
Same author

Entropy, Free Energy, and a Generalized Order Parameter for Liquid Crystal Phases of Chiral and Achiral Rods.

Journal of chemical theory and computation·2026
Same author

ER Stress-Mediated Impairment of Hepatic Lipid Export Drives Steatosis in AKI-Induced Remote Liver Injury.

Research square·2026

Related Experiment Video

Updated: Jan 10, 2026

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

69.7K

Morpheus: a fragment-based algorithm to predict fold-switching behaviour in proteins across proteomes.

Vijay Subramanian1,2, Rajeswari Appadurai2,3, Harikrishnan Venkatesh4

  • 1Indian Institute of Science Education and Research, Pune 411008, India.

Bioinformatics (Oxford, England)
|November 24, 2025
PubMed
Summary

Researchers developed Morpheus, a new algorithm to identify fold-switching proteins, which are proteins that change structure. This tool found that about 10% of proteins can fold-switch, expanding our understanding of the protein

More Related Videos

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.5K
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

909

Related Experiment Videos

Last Updated: Jan 10, 2026

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

69.7K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.5K
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

909

Area of Science:

  • Protein structure and dynamics
  • Computational biology
  • Bioinformatics

Background:

  • Fold-switching proteins, which deviate from classical folding models, are increasingly recognized as functionally important.
  • Accurate annotation of these proteins is crucial for understanding the full scope of the 'metamorphome'.

Purpose of the Study:

  • To develop and present Morpheus, a novel fragment-based classification approach for identifying fold-switching proteins from sequence data.
  • To analyze the structural diversity within protein sequences to predict fold-switching capabilities.

Main Methods:

  • Morpheus analyzes structural diversity using curated fragment data from the Protein Data Bank and AlphaFold Protein Structure Database.
  • The algorithm was applied to 57 proteomes, encompassing over 600,000 proteins.

Main Results:

  • Approximately 10% of the analyzed proteins were identified as having the ability to fold-switch.
  • A web server for Morpheus is available for testing user-defined sequences.

Conclusions:

  • The study highlights the prevalence of fold-switching proteins, suggesting they are more widespread than previously thought.
  • Morpheus provides a valuable tool for identifying fold-switching proteins and has implications for protein design and engineering.