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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.4K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.4K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.8K
2.8K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.4K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.4K
Protein Complex Assembly02:41

Protein Complex Assembly

16.7K
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...
16.7K
Protein Complex Assembly02:41

Protein Complex Assembly

2.6K
2.6K
Conservation of Protein Domains02:26

Conservation of Protein Domains

4.1K
4.1K

You might also read

Related Articles

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

Sort by
Same author

Two-year follow-up of a novel fully 3D-printed off-the-shelf humeral total shoulder arthroplasty prosthesis.

JSES international·2026
Same author

Within-household transmission risk of pulmonary tuberculosis in the era of universal antiretroviral therapy.

medRxiv : the preprint server for health sciences·2026
Same author

Motivation and pleasure deficits reflect altered network embedding of normal brain deviations in schizophrenia.

Schizophrenia research·2026
Same author

Targeting the H/KRAS α4-β6-α5 Allosteric Lobe with Macrocyclic Peptides.

ACS medicinal chemistry letters·2026
Same author

Cowpea mosaic virus as a candidate for intratumoral immunotherapy: progress, challenges, and future directions.

Advanced drug delivery reviews·2026
Same author

Regional HNSCC metabolomics reveals widespread changes to one-carbon metabolism and S-adenosylmethionine metabolism across tumour core, tumour edge and adjacent non-tumour tissues.

British journal of cancer·2026
Same journal

Gas-Responsive Metal-Organic Frameworks for Adaptive Thermal Energy Storage with Tunable Charge-Discharge Temperatures.

Journal of the American Chemical Society·2026
Same journal

Engineering a Thiamine-Dependent Benzoylformate Decarboxylase for Stereodivergent Radical C(sp<sup>3</sup>)-C(sp<sup>3</sup>) Bond Formation.

Journal of the American Chemical Society·2026
Same journal

Accelerated Directional Proton-Coupled Electron Transfer Enabled by Intrinsic Dipole Field in Biomimetic α-Helical Structure.

Journal of the American Chemical Society·2026
Same journal

Alternating Current-Driven Hydrogen Isotope Labeling of Aliphatic Amines Using 1,3-Propanedithiol as an Efficient Hydrogen Atom Transfer Reagent.

Journal of the American Chemical Society·2026
Same journal

Two-Dimensional van der Waals Polar Metal MoOBr<sub>2</sub>.

Journal of the American Chemical Society·2026
Same journal

Negatively Curved Chiral Bilayer Nanographene.

Journal of the American Chemical Society·2026
See all related articles

Related Experiment Video

Updated: Jan 29, 2026

Assembly and Characterization of Polyelectrolyte Complex Micelles
08:44

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

11.5K

Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain.

Sarah H Klass1, Matthew J Smith1, Tahoe A Fiala1

  • 1Department of Chemistry , University of California , Berkeley , California 94720 , United States.

Journal of the American Chemical Society
|February 12, 2019
PubMed
Summary
This summary is machine-generated.

Researchers developed novel fusion proteins that self-assemble into stable micelles, offering a biodegradable alternative to traditional surfactants for drug delivery and catalysis.

More Related Videos

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.4K

Related Experiment Videos

Last Updated: Jan 29, 2026

Assembly and Characterization of Polyelectrolyte Complex Micelles
08:44

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

11.5K
Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.4K

Area of Science:

  • Biomaterials Science
  • Polymer Chemistry
  • Protein Engineering

Background:

  • Diblock polymers self-assemble into micelles for encapsulating hydrophobic molecules.
  • Current surfactants often derive from non-renewable hydrocarbon sources.
  • There is a growing need for biodegradable, non-toxic, biologically synthesized alternatives.

Purpose of the Study:

  • To develop a new class of fusion proteins capable of self-assembling into stable micelles.
  • To investigate the properties and potential applications of these novel protein-based micelles.
  • To provide a sustainable, biomolecular alternative to conventional hydrocarbon-based surfactants.

Main Methods:

  • Designing fusion proteins based on a human intrinsically disordered protein with an appended hydrophobic segment.
  • Utilizing enzymatic cleavage of a solubilizing tag to induce micelle formation.
  • Characterizing micelle size (27 nm diameter) and formation conditions (pH, ionic strength, temperature).
  • Determining critical micelle concentration (CMC) and comparing it to sodium dodecyl sulfate (SDS).
  • Assessing the solubilization capacity for hydrophobic metal complexes and organic molecules.

Main Results:

  • Fusion proteins spontaneously self-assembled into stable micelles (27 nm diameter) upon enzymatic tag cleavage.
  • Micelle formation was robust across a wide range of pH, ionic strength, and temperature.
  • The critical micelle concentration (CMC) was in the low micromolar range, significantly lower than SDS.
  • The protein micelles effectively solubilized hydrophobic metal complexes and organic molecules.
  • The protein sequence design allows for encoding additional functionalities.

Conclusions:

  • A novel series of fusion proteins can self-assemble into stable, tunable micelles.
  • These protein-based micelles represent a promising biomolecular alternative to traditional surfactants.
  • Potential applications include catalysis and drug delivery, leveraging their solubilization capabilities and biodegradability.