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

Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

16.1K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
16.1K
Proteomics01:33

Proteomics

7.1K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
7.1K
Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

5.7K
Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such...
5.7K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.7K
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,...
5.7K
Protein Networks02:26

Protein Networks

3.9K
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,...
3.9K
Protein Complex Assembly02:41

Protein Complex Assembly

10.5K
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...
10.5K

You might also read

Related Articles

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

Sort by
Same author

Functional noncoding variants within the TBX1 enhancer contribute to tetralogy of Fallot.

Science China. Life sciences·2026
Same author

Corrigendum to: "Platelet ITGA2B inhibits caspase-8 and Rip3/Mlkl-dependent platelet death though PTPN6 during sepsis" [iScience, 26 (2023) 107414].

iScience·2026
Same author

Photopolymerizable placenta-derived ECM hydrogel enhances hUC-MSC-mediated wound healing via coordinated immunomodulation and angiogenesis.

Materials today. Bio·2026
Same author

Nature connectedness and healthy eating: The possible role of self-control.

Applied psychology. Health and well-being·2026
Same author

Lifetime Manipulation by Excitation Power in Lanthanide Core-Shell Nanocrystals Without Altering Composition.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same author

Synergistic texture enhancement of fibrous and amorphous fava bean protein fractions in reduced-phosphate myofibrillar protein gels: A concerted physical and chemical cross-linking mechanism.

Food chemistry·2026

Related Experiment Video

Updated: May 22, 2025

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

8.0K

Assembly and Functionality of 2D Protein Arrays.

Mingming Du1, Fanmeng Zeng1, YueFei Wang1

  • 1CAS Key Laboratory of Nano-Bio Interface, Division of Nanobiomedicine and i-Lab, Suzhou Institute of Nano-Tech and Nano-Bionics, Chinese Academy of Sciences, Suzhou, 215123, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|March 16, 2025
PubMed
Summary

Two-dimensional (2D) protein arrays offer unique stability and tunable properties. This review explores advancements in 2D protein assembly for novel functional biomaterials in diverse applications.

Keywords:
2D protein arraysbiomedical applicationsfunctional biomaterialsnanoparticlesself‐assembly

More Related Videos

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

17.9K
Flow-pattern Guided Fabrication of High-density Barcode Antibody Microarray
09:05

Flow-pattern Guided Fabrication of High-density Barcode Antibody Microarray

Published on: January 6, 2016

14.5K

Related Experiment Videos

Last Updated: May 22, 2025

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

8.0K
Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

17.9K
Flow-pattern Guided Fabrication of High-density Barcode Antibody Microarray
09:05

Flow-pattern Guided Fabrication of High-density Barcode Antibody Microarray

Published on: January 6, 2016

14.5K

Area of Science:

  • Materials Science
  • Nanotechnology
  • Biochemistry

Background:

  • Two-dimensional (2D) protein arrays are emerging nanomaterials with significant structural stability and tunable electronic/mechanical properties.
  • The field is driven by the goal to replicate and enhance natural protein system functionalities for advanced materials.
  • Understanding the fundamental principles of 2D protein self-assembly is crucial for developing novel functional biomaterials.

Purpose of the Study:

  • To review the current state of 2D protein nanotechnology.
  • To highlight methodologies for directing protein assembly into precise 2D architectures.
  • To emphasize the potential of 2D protein assemblies in next-generation biomaterials.

Main Methods:

  • Exploration of biological, chemical, and templated strategies for protein self-assembly.
  • Analysis of recent advancements in understanding protein self-assembly principles.
  • Assessment of techniques for integrating diverse components (small molecules, nanoparticles) into 2D protein arrays.

Main Results:

  • Development of sophisticated functional materials through precise 2D protein assembly.
  • Creation of highly ordered and intricate 2D protein patterns.
  • Enhanced material performance and versatility via integration of various components.

Conclusions:

  • 2D protein arrays represent a significant advancement in nanomaterials.
  • These assemblies offer transformative potential in biomedicine, catalysis, photosystems, and membrane filtration.
  • Continued research in protein self-assembly will drive innovation in functional biomaterials.