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 Modifications in the RER01:26

Protein Modifications in the RER

6.7K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
6.7K
Protein Folding01:22

Protein Folding

125.7K
Overview
125.7K
Protein Folding01:25

Protein Folding

10.8K
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...
10.8K
Protein and Protein Structure02:15

Protein and Protein Structure

86.4K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
86.4K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.8K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.8K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.1K
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...
19.1K

You might also read

Related Articles

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

Sort by
Same author

High-Performance Electrochemical Chloride Ion Storage with Hierarchical Ternary Metal Hydroxides for Sustainable Water Purification.

Advanced materials (Deerfield Beach, Fla.)·2025
Same author

Sex chromosomes/hormones and the tumor microenvironment of non-reproductive cancers.

Frontiers in immunology·2025
Same author

C-Reactive Protein Induces Immunosuppression by Activating FcγR2B in Pulmonary Macrophages to Promote Lung Metastasis.

Cancer research·2024
Same author

C-Reactive Protein Is Not the Driver Factor in Ulcerative Colitis.

Gastroenterology research and practice·2024
Same author

C-reactive protein: structure, function, regulation, and role in clinical diseases.

Frontiers in immunology·2024
Same author

Causal relationships between gut microbiota and dementia: A two-sample, bidirectional, Mendelian randomization study.

World journal of clinical cases·2024

Related Experiment Video

Updated: Jan 3, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

10.7K

Intra-subunit Disulfide Determines the Conversion and Structural Stability of CRP Isoforms.

Chun-Miao Zhang1, Yu-Bo Tan1, Hai-Hong Zhou2

  • 1MOE Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou, 730000, People's Republic of China.

Inflammation
|November 25, 2019
PubMed
Summary

C-reactive protein (CRP) transforms into monomeric CRP (mCRP) through a two-stage process involving subunit dissociation and aggregation. Reduction accelerates these changes, impacting mCRP

Keywords:
C-reactive proteindisulfideunfolding

More Related Videos

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

13.0K
High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

12.2K

Related Experiment Videos

Last Updated: Jan 3, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

10.7K
Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

13.0K
High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

12.2K

Area of Science:

  • Biochemistry
  • Immunology
  • Structural Biology

Background:

  • C-reactive protein (CRP) is a key human acute-phase reactant composed of five subunits.
  • CRP converts to monomeric CRP (mCRP) at inflammatory sites, enhancing its activity.
  • The conformational changes during CRP activation are not fully understood.

Purpose of the Study:

  • To investigate the conformational changes during CRP to mCRP conversion.
  • To examine the effect of reduction on CRP conformational changes.
  • To understand the role of electrostatic interactions in CRP structure.

Main Methods:

  • Circular dichroism spectroscopy
  • Fluorescence spectroscopy
  • Electron microscopy
  • Size-exclusion chromatography
  • Neoepitope expression

Main Results:

  • CRP conversion to mCRP is a two-stage process: subunit dissociation into molten globules, followed by aggregation.
  • Reduction accelerates molten globule formation and promotes more compact aggregates.
  • Electrostatic interactions significantly stabilize native CRP structure.

Conclusions:

  • The conformational changes in dissociated subunits and mCRP aggregation are critical for CRP's biological activities.
  • Understanding these structural dynamics provides insights into CRP's inflammatory roles.
  • This study elucidates the molecular mechanisms behind CRP activation.