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

87.0K
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...
87.0K
Antibody Structure01:10

Antibody Structure

65.4K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
65.4K
Ionic Crystal Structures02:42

Ionic Crystal Structures

16.9K
Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
Most monatomic ions behave as charged spheres, and their attraction for ions of opposite charge is the same in every direction. Consequently, stable structures for ionic compounds result (1) when ions of one charge are surrounded by as many ions as possible of the opposite...
16.9K
Structures of Solids02:22

Structures of Solids

17.5K
Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
17.5K
Structural Isomerism02:34

Structural Isomerism

21.5K
Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
Linkage isomers occur when the coordination compound contains a ligand that can bind to the transition metal center through two different atoms. For example, the CN− ligand can bind through the carbon atom or through the nitrogen atom. Similarly, SCN− can...
21.5K
Structure of Lipids03:38

Structure of Lipids

98.4K
Lipids include a diverse group of compounds that are largely nonpolar in nature. This is because they are hydrocarbons that include mostly nonpolar carbon-carbon or carbon-hydrogen bonds. Non-polar molecules are hydrophobic (“water fearing”), or insoluble in water. Lipids perform many different functions in a cell. Cells store energy for long-term use in the form of fats. Lipids also provide insulation from the environment for plants and animals. For example, they help keep aquatic...
98.4K

You might also read

Related Articles

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

Sort by
Same author

Structural basis of multimodal adsorption and infection initiation by <i>Vibrio</i> phage Peru-2.

bioRxiv : the preprint server for biology·2026
Same author

Integrated lipidomics and fatty acid positional distribution for nutritional assessment of nine mammalian milks.

NPJ science of food·2026
Same author

FlcE latches onto the FliL-stator complex to turbocharge flagellar motility in <i>Borrelia burgdorferi</i>.

bioRxiv : the preprint server for biology·2026
Same author

A New Era in Treponema pallidum Cultivation: Current Advances and Future Directions.

Sexually transmitted diseases·2026
Same author

Asymmetric architecture and adaptation of Treponema flagella.

Nature communications·2026
Same author

A Korean native halophyte extract attenuates the virulence of methicillin-resistant Staphylococcus aureus by inhibiting biofilm formation.

Scientific reports·2026

Related Experiment Video

Updated: Jan 22, 2026

Biophysical Characterization of Flagellar Motor Functions
06:08

Biophysical Characterization of Flagellar Motor Functions

Published on: January 18, 2017

8.6K

Structural insights into flagellar stator-rotor interactions.

Yunjie Chang1,2, Ki Hwan Moon1,3, Xiaowei Zhao2,4

  • 1Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, United States.

Elife
|July 18, 2019
PubMed
Summary
This summary is machine-generated.

The bacterial flagellar motor uses ion flux for rotation. In Borrelia burgdorferi, proton-driven torque causes a C-ring conformational change essential for flagellar movement.

Keywords:
bacterial flagellainfectious diseasemicrobiologymolecular biophysicsmotilitynanomachineprotein-protein interactionspirochetestructural biology

More Related Videos

Advanced Self-Healing Asphalt Reinforced by Graphene Structures: An Atomistic Insight
08:03

Advanced Self-Healing Asphalt Reinforced by Graphene Structures: An Atomistic Insight

Published on: May 31, 2022

5.6K
Fluorescence Lifetime Imaging of Molecular Rotors in Living Cells
09:45

Fluorescence Lifetime Imaging of Molecular Rotors in Living Cells

Published on: February 9, 2012

25.9K

Related Experiment Videos

Last Updated: Jan 22, 2026

Biophysical Characterization of Flagellar Motor Functions
06:08

Biophysical Characterization of Flagellar Motor Functions

Published on: January 18, 2017

8.6K
Advanced Self-Healing Asphalt Reinforced by Graphene Structures: An Atomistic Insight
08:03

Advanced Self-Healing Asphalt Reinforced by Graphene Structures: An Atomistic Insight

Published on: May 31, 2022

5.6K
Fluorescence Lifetime Imaging of Molecular Rotors in Living Cells
09:45

Fluorescence Lifetime Imaging of Molecular Rotors in Living Cells

Published on: February 9, 2012

25.9K

Area of Science:

  • Microbiology
  • Structural Biology
  • Biophysics

Background:

  • The bacterial flagellar motor is a complex molecular machine enabling motility.
  • Stator-rotor interaction and ion flux are critical for generating torque.
  • Understanding these mechanisms in pathogens like Borrelia burgdorferi is crucial.

Purpose of the Study:

  • To visualize the intact flagellar motor structure in Borrelia burgdorferi using cryo-electron tomography.
  • To elucidate the in situ localization and detailed interaction of the stator complex with the rotor.
  • To investigate the role of ion flux in driving conformational changes necessary for flagellar rotation.

Main Methods:

  • Cryo-electron tomography (cryo-ET) was utilized to image the native flagellar motor.
  • Structural analysis was performed on wild-type and stator-deletion mutants of Borrelia burgdorferi.
  • Comparative analysis focused on conformational changes in the C-ring.

Main Results:

  • The stator complex was localized in situ within the Borrelia burgdorferi flagellar motor.
  • Unprecedented detail of the stator-rotor interaction was revealed.
  • A conformational change in the flagella C-ring was observed, induced by stator-rotor interaction.
  • This conformational change was dependent on proton flux, as evidenced by non-motile mutants.

Conclusions:

  • Proton-driven torque is the primary driver of the conformational changes in the C-ring.
  • These conformational changes are essential for the torque generation required for flagellar rotation.
  • The findings provide new insights into the mechanics of bacterial motility in Borrelia burgdorferi.