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

12.0K
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...
12.0K
Protein Folding01:22

Protein Folding

129.6K
Overview
129.6K
Protein Folding01:22

Protein Folding

35.9K
35.9K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

20.6K
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...
20.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.3K
15.3K
The Unfolded Protein Response01:37

The Unfolded Protein Response

6.7K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
6.7K

You might also read

Related Articles

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

Sort by
Same author

Prevalence and Clinical Characteristics of Patients With Heart Failure With Preserved Ejection Fraction Who Meet the Obesity-Related Eligibility Criteria for Subcutaneous Incretin Receptor Agonists in Japan　- Insights From the PARACLETE Study.

Circulation journal : official journal of the Japanese Circulation Society·2026
Same author

Invasive Assessment of Coronary Microvascular Dysfunction in Patients With Wild-Type Transthyretin Amyloid Cardiomyopathy.

Journal of cardiac failure·2026
Same author

A novel risk score model for predicting mortality in heart failure with preserved ejection fraction: Insights from the CURE-HF Registry-ApHAC score.

PloS one·2025
Same author

Identification of Metabolomics Profile in Elderly Patients at the End Stage of Heart Failure.

Circulation journal : official journal of the Japanese Circulation Society·2025
Same author

Clinical Profile and Prognosis of Patients With Acute Decompensated Heart Failure Who Met the Obesity-Related Eligibility for Subcutaneous Semaglutide　- Findings From the CURE-HF Registry.

Circulation reports·2025
Same author

Clinical Utility of the HELT-E<sub>2</sub>S<sub>2</sub> Score for Risk Stratification in Patients with Acute Decompensated Heart Failure: Insights from the CURE-HF Registry.

Internal medicine (Tokyo, Japan)·2025

Related Experiment Video

Updated: Mar 11, 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

12.0K

Natively unfolded proteins: An overview.

Ken Nishikawa1

  • 1Department of Bioinformatics, Maebashi Institute of Technology, 460-1 Kamisadori, Maebashi, Gunma 371-0816, Japan.

Biophysics (Nagoya-Shi, Japan)
|November 19, 2016
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs), also known as natively unfolded proteins (NUPs), are crucial in cellular functions. This overview explores their prevalence, evolutionary significance, and reasons for delayed discovery in protein science.

Keywords:
disorder predictioneukaryoteintrinsic disorderstructural domaintranscription factor

More Related Videos

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.9K
Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

18.9K

Related Experiment Videos

Last Updated: Mar 11, 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

12.0K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.9K
Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

18.9K

Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology

Background:

  • Natively unfolded proteins (NUPs), or intrinsically disordered proteins, lack stable three-dimensional structures in vivo.
  • Their functional significance gained recognition following NMR studies and computational predictions indicating they constitute about one-third of eukaryotic proteins.

Approach:

  • This overview examines the historical context of NUP identification and discusses key questions surrounding their biological roles.
  • It explores the prevalence of NUPs across different life forms and their potential evolutionary implications.

Key Points:

  • Investigates the delayed recognition of NUPs as a significant area of protein science.
  • Addresses whether NUPs are exclusive to eukaryotes and the implications of their higher abundance in the nucleus.

Conclusions:

  • NUPs represent a substantial fraction of proteins, particularly in eukaryotes, and play vital roles.
  • Further research is needed to fully understand their evolutionary trajectory and functional diversity.