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 and Protein Structure02:15

Protein and Protein Structure

87.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
87.5K
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
No description available
2.6K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.9K
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...
2.9K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
No description available
2.1K
Structural Protein Function01:56

Structural Protein Function

29.9K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
29.9K

You might also read

Related Articles

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

Sort by
Same author

Black Hole Spectroscopy and Tests of General Relativity with GW250114.

Physical review letters·2026
Same author

First Evidence of Solar Neutrino Interactions on ^{13}C.

Physical review letters·2026
Same author

Measurement of Reactor Antineutrino Oscillation at SNO.

Physical review letters·2025
Same author

GW250114: Testing Hawking's Area Law and the Kerr Nature of Black Holes.

Physical review letters·2025
Same author

Improving cosmological reach of a gravitational wave observatory using Deep Loop Shaping.

Science (New York, N.Y.)·2025
Same author

The prevalence of hand pathology in regional orthopaedic hospitals in KwaZulu-Natal: A cross-sectional study.

South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde·2024

Related Experiment Video

Updated: Jan 31, 2026

Assembly and Characterization of Polyelectrolyte Complex Micelles
08:44

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

11.5K

Protein structures in SDS micelle-protein complexes.

W Parker1, P S Song

  • 1Department of Chemistry, University of Nebraska, Lincoln 68588-0304.

Biophysical Journal
|May 1, 1992
PubMed
Summary
This summary is machine-generated.

Sodium dodecyl sulfate (SDS) can induce ordered structures in proteins, contrary to its common use as a denaturing agent. This interaction reveals that many non-helical proteins can form amphiphilic structures when interacting with SDS micelles.

More Related Videos

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
08:46

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

Published on: January 6, 2015

33.6K
Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

24.8K

Related Experiment Videos

Last Updated: Jan 31, 2026

Assembly and Characterization of Polyelectrolyte Complex Micelles
08:44

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

11.5K
Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
08:46

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

Published on: January 6, 2015

33.6K
Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

24.8K

Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Molecular Biology

Background:

  • Sodium dodecyl sulfate (SDS) is a widely used detergent known for its protein denaturing properties.
  • Despite its denaturing role, SDS can induce ordered structures like alpha-helices and beta-sheets in certain peptides and proteins.
  • These SDS-induced structures are amphiphilic, possessing both hydrophobic and hydrophilic regions.

Purpose of the Study:

  • To investigate the interaction between SDS micelles and structurally diverse proteins.
  • To correlate the formation of SDS-induced structures with the presence of helical amphiphilic regions within protein sequences.
  • To explore the prevalence of induced amphiphilic structure formation in native non-ordered proteins.

Main Methods:

  • Analysis of protein-SDS micelle interactions.
  • Structural analysis of induced protein conformations.
  • Sequence analysis to identify amphiphilic regions.

Main Results:

  • SDS micelles induced ordered, amphiphilic structures in several structurally unrelated proteins.
  • A correlation was observed between the protein's primary sequence and the formation of these induced helical structures.
  • The study suggests that SDS-induced helical folding is a common phenomenon in proteins.

Conclusions:

  • The interaction of proteins with SDS micelles can lead to the formation of ordered amphiphilic structures.
  • The primary sequence of a protein plays a role in its ability to form SDS-induced structures.
  • Native, non-ordered protein structures commonly exhibit the ability to form induced amphiphilic ordered structures upon interaction with SDS.