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

Studying the Cytoskeleton01:17

Studying the Cytoskeleton

6.2K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
6.2K
Atomic Force Microscopy01:08

Atomic Force Microscopy

3.4K
Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
The probe is regarded as the heart of any AFM setup and comprises the...
3.4K

You might also read

Related Articles

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

Sort by
Same author

High-Speed Atomic Force Microscopy Reveals Aptamer-Mediated Conformational Trapping of METTL3-METTL14 for m<sup>6</sup>A Inhibition.

ACS applied materials & interfaces·2026
Same author

Large-Scale Structural Dynamics in the Tail Fiber Modulate the Infective Transition of the T7 Bacteriophage.

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

Structural Dynamics of the Afamin/Wnt3a Complex Mediated by the Afamin Hydrophobic Pocket.

Nano letters·2026
Same author

High-Speed Atomic Force Microscopy Reveals Disordered Region-Mediated Structural Plasticity of Anaplastic Lymphoma Kinase Fusion Proteins Induced by Inhibitors.

ACS nano·2026
Same author

Structural dynamics of mixed-subunit CaMKIIα/β heterododecamers filmed by high-speed AFM.

Nature communications·2025
Same author

Ligand Binding to the Membrane-Distal Domain of the Met Receptor Induces Dimerization at the Membrane-Proximal Domain.

ACS nano·2025

Related Experiment Video

Updated: Jul 2, 2025

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

7.3K

Observing Dynamic Conformational Changes within the Coiled-Coil Domain of Different Laminin Isoforms Using High-Speed

Lucky Akter1, Holger Flechsig1, Arin Marchesi1,2

  • 1WPI Nano Life Science Institute, Kanazawa University, Kanazawa 920-1167, Japan.

International Journal of Molecular Sciences
|February 24, 2024
PubMed
Summary

High-speed atomic force microscopy visualized dynamic structural changes in laminin-111 and laminin-332. This revealed distinct coiled-coil domain flexibility and C-terminal globular domain rearrangements in these crucial cell adhesion proteins.

Keywords:
HS-AFMcoiled-coilextracellular matrixlaminin-111laminin-332laminin-511molecular dynamics

More Related Videos

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
06:56

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

1.0K
Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

2.6K

Related Experiment Videos

Last Updated: Jul 2, 2025

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

7.3K
Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
06:56

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

1.0K
Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

2.6K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Laminins are essential extracellular matrix glycoproteins involved in cell adhesion and tissue organization.
  • Their cross-shaped structure comprises α, ß, and γ-chains, with laminin G-like (LG) domains at the C-terminus mediating cell binding.
  • Previous studies suggested dynamic conformational changes regulate laminin function, but lacked single-molecule dynamic analysis.

Purpose of the Study:

  • To investigate the dynamic conformational changes of laminin-111 and laminin-332 at the single-molecule level.
  • To characterize the ultrastructure and conformational flexibility of laminin coiled-coil and LG domains under physiological conditions.
  • To provide novel insights into laminin molecular dynamics using high-speed atomic force microscopy.

Main Methods:

  • High-speed atomic force microscopy (HS-AFM) was employed for real-time, sub-second imaging of laminin-111 and laminin-332.
  • Surface immobilization and imaging conditions were optimized for high-resolution visualization.
  • Complementary computational methods including AlphaFold structure prediction and molecular dynamics simulations were utilized.

Main Results:

  • Laminin-111 exhibited a stable, S-shaped coiled-coil domain with minimal conformational changes.
  • Laminin-332 displayed rapid switching of its coiled-coil domain between straight and bent conformations around a central hinge.
  • Dynamic rearrangements of C-terminal LG domains between compact and open states were observed for both laminin isoforms.

Conclusions:

  • HS-AFM directly visualizes dynamic molecular rearrangements in laminin isoforms, offering unprecedented structural insights.
  • Laminin-332 possesses a flexible coiled-coil domain, suggesting a distinct mechanism for regulating its function compared to laminin-111.
  • The study highlights the importance of dynamic conformational changes in laminin function and provides a powerful technique for their analysis.