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

127.9K
Overview
127.9K
Protein Folding01:25

Protein Folding

11.5K
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...
11.5K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.6K
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...
19.6K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.8K
2.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.8K
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...
19.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.0K
15.0K

You might also read

Related Articles

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

Sort by
Same author

Leveraging paired germline and somatic analysis to improve the classification of DDX41 variants.

British journal of haematology·2026
Same author

Long-term outcomes of metabolic and bariatric surgery: a 10-year study of effectiveness and predictors.

International journal of obesity (2005)·2026
Same author

Incidentally vs nonincidentally diagnosed paragangliomas: Experience of a tertiary referral center.

Endocrinologia, diabetes y nutricion·2026
Same author

Microenvironmental TGF-β is an early driver of NF1-associated tumor formation.

Cell reports·2026
Same author

Semen analysis as a biomarker of male aging: biological mechanisms, clinical implications, and public health perspectives.

Human reproduction (Oxford, England)·2025
Same author

Ten-Year Weight Regain after Bariatric Surgery: Prevalence, Predictors, and Metabolic Impact.

Obesity facts·2025

Related Experiment Video

Updated: Feb 7, 2026

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

11.9K

Protein folding and quinary interactions: creating cellular organisation through functional disorder.

Sara Ribeiro1, Simon Ebbinghaus2, João C Marcos1

  • 1Centre of Chemistry, University of Minho, Braga, Portugal.

FEBS Letters
|August 3, 2018
PubMed
Summary

Quinary interactions can destabilize globular proteins, creating functional partially unfolded states. This mechanism is relevant to intracellular organization, phase separation, and stress responses.

Keywords:
intracellular organisationmacromolecular crowdingmembraneless organellesphase separationprotein stability

More Related Videos

Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

13.2K
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

8.5K

Related Experiment Videos

Last Updated: Feb 7, 2026

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

11.9K
Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

13.2K
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

8.5K

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biophysics

Background:

  • Marginal protein stability is governed by excluded volume and soft interactions.
  • Quinary interactions, a type of soft interaction, influence protein stability and cellular organization.
  • Proteins exhibit structural flexibility and can exist in multiple functional states.

Purpose of the Study:

  • To propose that quinary interactions can induce functional partially unfolded protein states.
  • To explore the biological relevance of quinary-induced protein destabilization.

Main Methods:

  • Theoretical analysis of protein stability.
  • Review of existing literature on quinary interactions and protein flexibility.

Main Results:

  • Quinary interactions can sufficiently destabilize globular proteins to form functional partially unfolded states.
  • This mechanism offers a new perspective on protein structural dynamics.

Conclusions:

  • Quinary-induced protein destabilization is a viable mechanism for generating functional partially unfolded states.
  • This process has implications for intracellular phase separation and stress response pathways.