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

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...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview

You might also read

Related Articles

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

Sort by
Same author

The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture.

Nature microbiology·2026
Same author

Fluorescence Correlation Spectroscopy to Examine Protein-Lipid Interactions in Membranes.

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

Force patterning drives quasistratification and graded tissue-scale spatial order in auditory epithelia.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Ion- and Temperature-Programmable Reconfiguration of Subcompartments in Synthetic Cells.

Chembiochem : a European journal of chemical biology·2026
Same author

Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape.

Science (New York, N.Y.)·2026
Same author

Optimizing spatial organization of FtsZ rings for large-scale constriction in synthetic cells.

Nature communications·2026

Related Experiment Video

Updated: Jun 2, 2026

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
08:10

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

Published on: July 28, 2018

Protein self-organization: lessons from the min system.

Martin Loose1, Karsten Kruse, Petra Schwille

  • 1Biophysics, BIOTEC, Dresden University of Technology, Dresden, Germany. petra.schwille@biotec.tu-dresden.de

Annual Review of Biophysics
|May 7, 2011
PubMed
Summary

Biological systems self-organize, but complexity hinders study. Researchers are exploring minimal systems like Min protein oscillations in E. coli for insights into intracellular organization and pattern formation.

More Related Videos

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

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

Related Experiment Videos

Last Updated: Jun 2, 2026

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
08:10

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

Published on: July 28, 2018

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

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

Area of Science:

  • Biophysics
  • Cell Biology
  • Systems Biology

Background:

  • Biological systems exhibit complex self-organization across scales.
  • Studying self-organization is challenging due to biological complexity.
  • Minimal biological systems offer a promising avenue for understanding emergent behavior.

Purpose of the Study:

  • To review the current understanding of Min protein self-organization in Escherichia coli.
  • To explore the in vivo and in vitro mechanisms of Min protein oscillations.
  • To discuss the potential of Min oscillations for intracellular organization and cell geometry sensing.

Main Methods:

  • Review of existing literature on Min protein dynamics.
  • Analysis of in vivo and in vitro experimental data.
  • Theoretical modeling of protein self-organization and pattern formation.

Main Results:

  • Min protein oscillations in E. coli are a well-understood example of protein self-organization.
  • These oscillations have been successfully reconstituted in vitro.
  • The Min system demonstrates potential for sensing cellular geometry.

Conclusions:

  • Min protein oscillations represent a fundamental mechanism for intracellular organization.
  • Spontaneous protein waves may be a general principle for pattern formation in cells.
  • Cooperative membrane interactions, potentially energy-dependent, could regulate these oscillations.