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

128.0K
Overview
128.0K
Protein Folding01:25

Protein Folding

11.6K
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...
11.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.9K
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...
19.9K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.1K
No description available
15.1K
Regulated Protein Degradation02:58

Regulated Protein Degradation

8.9K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
8.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.7K

You might also read

Related Articles

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

Sort by
Same author

Prenatal Exposure to PFOA Induces Ovarian Function Impairment via the Disruption of the PPARγ/ANGPTL4 Pathway.

Environment & health (Washington, D.C.)·2026
Same author

Integrated model of Student Standardized Patients and peer assessment enhances SOAP note proficiency in obstetrics and gynecology residency.

Frontiers in medicine·2026
Same author

Piezo-metastructured arrays enhance osteoblast mitochondrial quality control to promote osseointegration under osteoporotic conditions.

Biomaterials·2026
Same author

Smart molecular design for functional cellulose gels and flexible devices.

Smart molecules : open access·2026
Same author

Proteolytic Imbalance of the MMP/E-Cadherin Axis in Genitourinary Syndrome of Menopause: A Cross-Sectional Study.

International journal of women's health·2026
Same author

Thyroid Hormone in Women with Premature Ovarian Insufficiency: A Case-Control Study.

International journal of women's health·2026
Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026
Same journal

Multifaceted effects of N-glycosylation on amyloidogenic κ light chains in AL amyloidosis.

Structure (London, England : 1993)·2026
Same journal

Near-complete cryo-EM structure of the Klebsiella pneumoniae podophage RAN69 reveals tail fiber-spike interface and a divergent pre-ejectosome.

Structure (London, England : 1993)·2026
Same journal

Saxiphilin is a broad-spectrum toxin sponge for C13-modified saxitoxins.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of YfdQ reveals a widespread family of bacteriophage-associated proteins with shell-like assemblies.

Structure (London, England : 1993)·2026
See all related articles

Related Experiment Video

Updated: Feb 9, 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

Regulating Protein Function by Delayed Folding.

Jianhong Zhou1, A Keith Dunker1

  • 1Center for Computational Biology and Bioinformatics, Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.

Structure (London, England : 1993)
|May 3, 2018
PubMed
Summary
This summary is machine-generated.

Many secreted proteins exhibit delayed folding, forming long-lived, loosely packed intermediates. This protein folding characteristic is linked to increased disorder and reduced hydrophobicity, with signal peptides playing a stabilizing role.

More Related Videos

Trans-vivo Delayed Type Hypersensitivity Assay for Antigen Specific Regulation
11:49

Trans-vivo Delayed Type Hypersensitivity Assay for Antigen Specific Regulation

Published on: May 2, 2013

16.7K
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

Related Experiment Videos

Last Updated: Feb 9, 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
Trans-vivo Delayed Type Hypersensitivity Assay for Antigen Specific Regulation
11:49

Trans-vivo Delayed Type Hypersensitivity Assay for Antigen Specific Regulation

Published on: May 2, 2013

16.7K
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

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Protein folding is crucial for cellular function.
  • Secreted proteins navigate the secretory pathway before reaching their final destination.
  • Understanding the folding dynamics of secreted proteins is essential for cell biology.

Purpose of the Study:

  • To investigate the folding mechanisms of secreted proteins.
  • To characterize the structural properties of secreted protein folding intermediates.
  • To explore the role of signal peptides in protein folding.

Main Methods:

  • Bioinformatics analysis of protein sequences and structures.
  • Biophysical techniques to study protein folding dynamics.
  • Computational modeling of protein folding pathways.

Main Results:

  • Many secreted proteins form long-lived, loosely packed folding intermediates.
  • These intermediates exhibit higher levels of disorder and lower hydrophobicity compared to structured cytosolic proteins.
  • Signal peptides appear to stabilize these folding intermediates through unelucidated mechanisms.

Conclusions:

  • Secreted proteins may adopt distinct folding pathways involving stable, disordered intermediates.
  • Signal peptides are implicated in modulating the folding kinetics and stability of secreted proteins.
  • Further research is needed to fully understand the mechanisms by which signal peptides influence protein folding.