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 Complex Assembly02:41

Protein Complex Assembly

16.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.5K
Protein Complex Assembly02:41

Protein Complex Assembly

2.5K
2.5K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.4K
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,...
6.4K
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
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
2.1K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

5.5K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
5.5K

You might also read

Related Articles

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

Sort by
Same author

DAQplugin: Deep Learning based Real-time Model Evaluation Plugin for ChimeraX.

bioRxiv : the preprint server for biology·2026
Same author

Direct Detection and Atomic Modeling of Ligands in Cryo-EM Maps Using Deep Learning.

bioRxiv : the preprint server for biology·2026
Same author

On the state of protein function prediction: a report on the fourth CAFA challenge.

bioRxiv : the preprint server for biology·2026
Same author

PL-PatchSurfer3: improved structure-based virtual screening for structure variation using 3D Zernike descriptors.

Journal of cheminformatics·2026
Same author

Multivalent recognition of ferritin by full-length NCOA4 enables robust ferritinophagy.

Protein science : a publication of the Protein Society·2026
Same author

MVGFormer: Multi-view perspective with graph-guided transformer for cryo-ET segmentation.

Knowledge-based systems·2026
Same journal

Isolation of Mesenchymal Stem Cell-Derived Extracellular Vesicles.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Modeling Melanoma Immune Surveillance by CAR-T Cells in Human Skin Organoids.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Stepwise Optimization of a Matrigel-Based In Vitro Angiogenesis Assay for Reproducible and Quantifiable 2D-Tube Formation Using HUVECs.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Quantifying Mechanical Properties of Fresh Ovarian Tissue with Optical Brillouin Microscopy.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

3D Chromatin Architecture During Early Development: New Methods and New Findings.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Metabolic Plasticity in Embryogenesis Throughout the Lens of NAD<sup></sup>.

Methods in molecular biology (Clifton, N.J.)·2026
See all related articles

Related Experiment Video

Updated: Jan 6, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.4K

Path-LZerD: Predicting Assembly Order of Multimeric Protein Complexes.

Genki Terashi1, Charles Christoffer2, Daisuke Kihara3,4

  • 1Department of Biological Sciences, Purdue University, West Lafayette, IN, USA.

Methods in Molecular Biology (Clifton, N.J.)
|October 5, 2019
PubMed
Summary
This summary is machine-generated.

Understanding how multi-protein complexes assemble is crucial for cell function and drug design. We developed Path-LZerD, a computational tool that simulates protein complex assembly, offering an efficient alternative to resource-intensive experimental methods.

Keywords:
Assembly orderMultimeric protein complexPPIPPI networkProtein dockingProtein structure modelingProtein–protein interactionStructure prediction

More Related Videos

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

7.0K
Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

20.3K

Related Experiment Videos

Last Updated: Jan 6, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.4K
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

7.0K
Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

20.3K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Computational Biology

Background:

  • Protein complexes with multiple subunits perform vital cellular functions.
  • Understanding protein complex assembly pathways is key for molecular mechanisms, drug design, and protein engineering.
  • Experimental methods for determining assembly paths are often resource-intensive.

Purpose of the Study:

  • To introduce and explain the usage of the Path-LZerD software.
  • To demonstrate a computational approach for predicting protein complex assembly pathways.
  • To provide a foundation for artificial design of protein complexes and drug development.

Main Methods:

  • Development of a computational method named Path-LZerD.
  • Simulation of the protein complex docking process to predict assembly pathways.
  • Explanation of software usage with practical examples.

Main Results:

  • Path-LZerD successfully predicts the assembly path of protein complexes.
  • The computational method provides an efficient alternative to experimental approaches.
  • The software enables detailed insights into the molecular mechanisms of complex formation.

Conclusions:

  • Path-LZerD offers a valuable computational tool for studying protein complex assembly.
  • This method facilitates research in structural biology, drug discovery, and protein design.
  • The software serves as a foundation for future advancements in understanding and manipulating protein complex formation.