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 Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...

You might also read

Related Articles

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

Sort by
Same author

Exome-wide association study of blood lipids in 1,158,017 individuals from diverse populations.

Nature genetics·2026
Same author

Mendelian Randomization Suggests a Causal Link Between Glycemic Traits and Thoracic Aortic Structures and Diseases.

JACC. Basic to translational science·2025
Same author

Conformation-gated binding underlies kinetic asymmetry and negative cooperativity in ATP:cob(I)alamin adenosyltransferase.

Cell reports. Physical science·2025
Same author

Multipopulation GWAS for venous thromboembolism identifies novel loci followed by experimental validation in zebrafish.

Blood advances·2025
Same author

Genome-wide association study and multi-ancestry meta-analysis identify common variants associated with carotid artery intima-media thickness.

medRxiv : the preprint server for health sciences·2025
Same author

Dissecting the Genetic Architecture of Intracranial Aneurysms.

Circulation. Genomic and precision medicine·2025

Related Experiment Video

Updated: May 22, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Dynamic multibody protein interactions suggest versatile pathways for copper trafficking.

Aaron M Keller1, Jaime J Benítez, Derek Klarin

  • 1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.

Journal of the American Chemical Society
|May 15, 2012
PubMed
Summary
This summary is machine-generated.

The human copper chaperone Hah1 delivers copper to Wilson

More Related Videos

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
11:38

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

Related Experiment Videos

Last Updated: May 22, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
11:38

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

Area of Science:

  • Biochemistry and Molecular Biology
  • Intracellular Copper Transport Mechanisms

Background:

  • The human copper chaperone Hah1 facilitates intracellular copper (Cu+) delivery to the Wilson's Disease Protein (WDP).
  • WDP possesses six metal-binding domains (MBDs) that receive Cu+ from Hah1, but the role of multiple MBDs in copper trafficking remains unclear.
  • Previous research explored Hah1 interactions with isolated WDP MBDs.

Purpose of the Study:

  • To investigate the interaction dynamics between Hah1 and a double-domain WDP construct (MBD34).
  • To understand how Hah1 interacts with multiple MBDs within the WDP multidomain system.
  • To elucidate the functional significance of MBD multiplicity in copper trafficking.

Main Methods:

  • Employed single-molecule fluorescence resonance energy transfer (smFRET) combined with vesicle trapping.
  • Systematically probed Hah1-MBD3, Hah1-MBD4, and intramolecular MBD3-MBD4 interaction dynamics.
  • Utilized alternating donor and acceptor positions to analyze interaction geometries.

Main Results:

  • Observed conserved interconverting interaction geometries in both intermolecular Hah1-MBD and intramolecular MBD-MBD interactions.
  • Found that Hah1-MBD interactions within the MBD34 construct are stabilized by an order of magnitude compared to isolated single-MBDs.
  • Gathered thermodynamic and kinetic evidence indicating Hah1 can simultaneously interact with both MBD3 and MBD4.

Conclusions:

  • The enhanced interaction stability of Hah1 with the multi-MBD system suggests a more robust copper delivery mechanism.
  • Dynamic intramolecular MBD-MBD interactions contribute to the versatility of copper trafficking.
  • Hah1's capacity for simultaneous interaction with multiple WDP MBDs points to an efficient and adaptable Hah1-to-WDP copper transport pathway.