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 Experiment Videos

Kinesin from pig brain studied by electron microscopy.

L A Amos1

  • 1MRC Laboratory of Molecular Biology, Cambridge, UK.

Journal of Cell Science
|February 1, 1987
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Molecular motors: not quite like clockwork.

Cellular and molecular life sciences : CMLS·2008
Same author

3D electron microscopy of the interaction of kinesin with tubulin.

Cell structure and function·2004
Same author

Prokaryotic origin of the actin cytoskeleton.

Nature·2001
Same author

Antibodies to cytoplasmic dynein heavy chain map the surface and inhibit motility.

Journal of molecular biology·2001
Same author

Three-dimensional structure of motor molecules.

Cellular and molecular life sciences : CMLS·2001
Same author

Helical tubes of FtsZ from Methanococcus jannaschii.

Biological chemistry·2000

Researchers purified kinesin, a motor protein, from pig brains. Electron microscopy revealed its structure and how it attaches to microtubules, crucial for intracellular transport.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Kinesin is a vital motor protein responsible for intracellular transport along microtubule tracks.
  • Understanding kinesin's structure and function is key to deciphering cellular mechanics.

Purpose of the Study:

  • To purify and structurally characterize kinesin from pig brain.
  • To investigate the binding interactions of kinesin with microtubules.

Main Methods:

  • Purification of kinesin using established protocols.
  • Structural analysis via electron microscopy (shadowed and negative staining).

Main Results:

  • Kinesin visualized as a ~100 nm rod with distinct branched and forked ends.

Related Experiment Videos

  • A potential flexible joint observed near the middle of the kinesin molecule.
  • Kinesin demonstrated attachment to microtubules via its forked end (in presence of AMP.PNP) or branched end, occasionally cross-linking microtubules.

    • Conclusions:

    • The study provides detailed structural insights into purified pig brain kinesin.
    • Kinesin exhibits versatile binding modes to microtubules, suggesting complex transport mechanisms.