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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.3K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.3K
Crystal Field Theory - Octahedral Complexes02:58

Crystal Field Theory - Octahedral Complexes

28.4K
Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
CFT focuses on...
28.4K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.2K
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....
8.2K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.6K
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...
5.6K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

4.4K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.4K

You might also read

Related Articles

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

Sort by
Same author

Recent Trends in Metabolomics by NMR Spectroscopy.

Angewandte Chemie (International ed. in English)·2026
Same author

Structural biology of ferritin nanocages.

FEBS letters·2026
Same author

An Integrated NMR Approach for Evaluating Linker-Payload Conjugation with Monoclonal Antibodies.

Bioconjugate chemistry·2026
Same author

S1P<sub>3</sub> Receptor Mediates the Proinflammatory Effect of the Endocannabinoid 2-Arachidonoylglycerol in Endometriotic Epithelial Cells.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2025
Same author

Ferritin-assisted biomineralization and drug delivery: It's a matter of hard and soft.

Journal of inorganic biochemistry·2025
Same author

Design of 2-Aminobenzothiazole Derivatives Targeting Trypanosomatid PTR1 by a Multidisciplinary Fragment Hybridization Approach.

Journal of medicinal chemistry·2025

Related Experiment Video

Updated: Apr 25, 2026

Electrophoretic Mobility Shift Assay EMSA for the Study of RNA-Protein Interactions: The IRE/IRP Example
12:44

Electrophoretic Mobility Shift Assay EMSA for the Study of RNA-Protein Interactions: The IRE/IRP Example

Published on: December 3, 2014

53.4K

Loop electrostatics modulates the intersubunit interactions in ferritin.

Caterina Bernacchioni1, Veronica Ghini, Cecilia Pozzi

  • 1Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.

ACS Chemical Biology
|August 23, 2014
PubMed
Summary

Electrostatic interactions, specifically salt bridges between Asp80 and Lys82 in ferritin L-loops, are crucial for nanocage self-assembly. Modifying these residues inhibits assembly, impacting ferritin structure and stability.

More Related Videos

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

1.4K
Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells
10:23

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Published on: December 13, 2016

11.3K

Related Experiment Videos

Last Updated: Apr 25, 2026

Electrophoretic Mobility Shift Assay EMSA for the Study of RNA-Protein Interactions: The IRE/IRP Example
12:44

Electrophoretic Mobility Shift Assay EMSA for the Study of RNA-Protein Interactions: The IRE/IRP Example

Published on: December 3, 2014

53.4K
Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

1.4K
Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells
10:23

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Published on: December 13, 2016

11.3K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Ferritin forms 24-mer nanocages via subunit self-assembly.
  • Intersubunit contacts, including L-loop interactions, stabilize the cage structure.
  • Salt bridges between Asp80 and Lys82 are key anchor points in L-loop interactions.

Purpose of the Study:

  • To investigate the role of electrostatic interactions in ferritin nanocage self-assembly.
  • To analyze the impact of specific residue substitutions on ferritin assembly and stability.
  • To elucidate the kinetic role of L-loop electrostatic pairing in ferritin quaternary structure formation.

Main Methods:

  • Site-directed mutagenesis to substitute Asp80 with Lys (D80K) and introduce multiple Lys residues (D80KI81K).
  • Overexpression in E. coli to assess subunit oligomerization and nanocage formation.
  • Analysis of protein solubility, thermal stability, and crystallization properties.
  • 3D structure determination of the D80K variant.

Main Results:

  • Substitution of Asp80 with Lys (D80K) introduced electrostatic repulsions, inhibiting subunit oligomerization and leading to inclusion body formation.
  • Slower expression conditions allowed formation of functional D80K nanocages.
  • The D80K variant exhibited altered solubility and crystallized in a low-density packing.
  • Introducing three contiguous Lys residues (D80KI81K) further inhibited assembly, reducing solubility and thermal stability.
  • The 3D structure of D80K was similar to wild type, with altered side chain orientations.

Conclusions:

  • Electrostatic pairing at the center of L-loops plays a critical kinetic role in ferritin nanocage self-assembly.
  • Disruption of these salt bridges significantly hinders or prevents nanocage formation.
  • Understanding these interactions provides insights into protein self-assembly mechanisms and potential for protein engineering.