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 Folding01:25

Protein Folding

8.2K
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...
8.2K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.1K
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...
18.1K
Amyloid Fibrils03:03

Amyloid Fibrils

9.6K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.6K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

40
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
40
Protein Organization01:13

Protein Organization

138.7K
Overview
138.7K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.0K
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...
11.0K

You might also read

Related Articles

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

Sort by
Same author

Atypical GPCR Activation Resolved by Nanobody Engineering.

bioRxiv : the preprint server for biology·2026
Same author

Explaining how mutations affect AlphaFold predictions.

bioRxiv : the preprint server for biology·2026
Same author

Biosafety assessment of engineered CCL20 locked dimers in vivo.

Cell biology and toxicology·2025
Same author

Constitutive activity of an atypical chemokine receptor revealed by inverse agonistic nanobodies.

Nature communications·2025
Same author

Progress toward new function and design of extracellular G protein-coupled receptor nanobodies.

Molecular pharmacology·2025
Same author

Chemokines kill bacteria without triggering antimicrobial resistance by binding anionic phospholipids.

Science advances·2025
Same journal

Metabolic control of RNA splicing by polyamines.

Trends in biochemical sciences·2026
Same journal

The role of glycan modifications in health and disease.

Trends in biochemical sciences·2026
Same journal

Strengthening the philosophical basis of graduate science education.

Trends in biochemical sciences·2026
Same journal

CycloPepper learns cyclization sites in therapeutic peptides.

Trends in biochemical sciences·2026
Same journal

Glycosphingolipids in cell identity: Biosynthesis, functions, and emerging tools.

Trends in biochemical sciences·2026
Same journal

Cap in hand: giant viruses, stolen translation, and a road to endosymbiosis?

Trends in biochemical sciences·2026
See all related articles

Related Experiment Video

Updated: Jul 28, 2025

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
12:38

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

6.1K

Metamorphic protein folding as evolutionary adaptation.

Acacia F Dishman1, Brian F Volkman2

  • 1Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA; Medical Scientist Training Program, Medical College of Wisconsin, Milwaukee, WI 53226, USA.

Trends in Biochemical Sciences
|June 3, 2023
PubMed
Summary
This summary is machine-generated.

Metamorphic proteins reversibly switch between stable structures, challenging the

Keywords:
adaptive traitancestral sequence reconstructionfold-switching proteinprotein fitnessthermodynamic hypothesis

More Related Videos

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

11.3K
Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.0K

Related Experiment Videos

Last Updated: Jul 28, 2025

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
12:38

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

6.1K
Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

11.3K
Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.0K

Area of Science:

  • Protein biochemistry
  • Evolutionary biology
  • Structural biology

Background:

  • Metamorphic proteins exhibit reversible structural switching, previously considered evolutionary intermediates.
  • The 'one sequence, one fold' paradigm was challenged by these proteins.
  • Examples like the NusG family and chemokine XCL1 highlight their significance.

Purpose of the Study:

  • To investigate the evolutionary role and prevalence of metamorphic proteins.
  • To determine if metamorphic folding is an adaptive trait rather than a transient evolutionary stage.
  • To explore the sequence space compatible with metamorphic protein structures.

Main Methods:

  • Analysis of extant protein families.
  • Resurrection of ancestral protein sequences.
  • Bioinformatic analysis of protein sequence space.

Main Results:

  • Evidence suggests metamorphic folding is an adaptive evolutionary feature.
  • Large sequence spaces are compatible with metamorphic protein structures.
  • NusG family and chemokine XCL1 exemplify optimized metamorphic proteins.

Conclusions:

  • Metamorphic proteins are likely preserved and optimized for biological fitness.
  • Fold switching in metamorphic proteins enables diverse biological functions.
  • Metamorphic proteins may be more widespread than previously assumed.