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Related Concept Videos

Atomic Force Microscopy01:08

Atomic Force Microscopy

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...
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

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...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...

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Related Experiment Video

Updated: Jun 8, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

Imaging collagen II using atomic force microscopy (AFM).

Marija Plodinec, Marko Loparic, Ueli Aebi

    Cold Spring Harbor Protocols
    |October 5, 2010
    PubMed
    Summary
    This summary is machine-generated.

    This study details atomic force microscopy (AFM) methods for analyzing collagen II self-assembly. Researchers visualize tropocollagen subunit organization and fibril formation in cartilage extracellular matrix.

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    Area of Science:

    • Biochemistry
    • Biophysics
    • Materials Science

    Background:

    • Collagen II is a fibrous protein crucial for cartilage structure.
    • Tropocollagen subunits self-assemble into microfibrils and then larger collagen fibrils.
    • These fibrils exhibit a characteristic 67-nm repeat due to molecular staggering.

    Purpose of the Study:

    • To present a protocol for preparing collagen protein samples for Atomic Force Microscopy (AFM).
    • To demonstrate the generation of AFM images for analyzing collagen self-assembly.
    • To study the structural organization of collagen during self-assembly.

    Main Methods:

    • Sample preparation for collagen protein analysis.
    • Atomic Force Microscopy (AFM) imaging techniques.
    • In-situ and post-manipulation imaging of collagen samples.

    Main Results:

    • Successful preparation of collagen samples for AFM analysis.
    • Generation of high-resolution AFM images detailing collagen fibril formation.
    • Visualization of tropocollagen subunit assembly into microfibrils and fibrils.

    Conclusions:

    • AFM is a suitable technique for visualizing collagen self-assembly.
    • The protocol enables detailed structural analysis of collagen fibril formation.
    • Understanding collagen assembly is vital for cartilage tissue engineering and research.