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

Nebulin, a helical actin binding protein

M Pfuhl1, S J Winder, A Pastore

  • 1EMBL Heidelberg, Germany.

The EMBO Journal
|April 15, 1994
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

First Measurement of Time-Dependent CP Violation in the Flavor-Changing Neutral-Current Decay B^{0}→K_{S}^{0}μ^{+}μ^{-}.

Physical review letters·2026
Same author

Measurement of the Top-Quark Production Cross Section and Charge Asymmetry at LHCb.

Physical review letters·2026
Same author

Searches for B^{0}→K^{+}π^{-}τ^{+}τ^{-} and B_{s}^{0}→K^{+}K^{-}τ^{+}τ^{-} Decays.

Physical review letters·2026
Same author

First Evidence of the B_{s}^{0}→K^{-}π^{+}γ Decay.

Physical review letters·2026
Same author

Precision Measurement of CP Violation and Branching Fractions in B^{±}→K_{S}^{0}h^{±} (h=π, K) Decays and Search for the Rare Decay B_{c}^{±}→K_{S}^{0}K^{±}.

Physical review letters·2026
Same author

First Observation of the B[over ¯]_{s}^{0}→Λ_{c}^{+}Λ[over ¯]_{c}^{-} Decay and Evidence for the B[over ¯]^{0}→Λ_{c}^{+}Λ[over ¯]_{c}^{-} Decay.

Physical review letters·2026
Same journal

Chromosome condensation mechanically primes the nucleus for mitosis.

The EMBO journal·2026
Same journal

NDR kinase SAX-1 controls dendrite branch-specific elimination during neuronal remodeling in C. elegans.

The EMBO journal·2026
Same journal

Assembly of the catalytic module and the rotor of human ATP synthase.

The EMBO journal·2026
Same journal

Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC.

The EMBO journal·2026
Same journal

Conformational changes of the baseplate regulating tail contraction of Staphylococcus phage 812.

The EMBO journal·2026
Same journal

Cellular assembly and functional resilience of the mammalian RNA exosome.

The EMBO journal·2026
See all related articles

Nebulin repeats are the smallest unit for actin interaction, forming a helical structure that stabilizes in the presence of negative charges, crucial for thin filament regulation in skeletal muscle.

Area of Science:

  • Muscle physiology
  • Protein biochemistry
  • Structural biology

Background:

  • Nebulin is a giant skeletal muscle protein.
  • It is proposed to regulate thin filament length.
  • Nebulin consists of repeating units of ~35 amino acids.

Purpose of the Study:

  • Characterize conformational and functional properties of nebulin repeats.
  • Determine the smallest unit of nebulin-actin interaction.
  • Propose a structural model for the F-actin-nebulin complex.

Main Methods:

  • Circular dichroism spectroscopy
  • Nuclear magnetic resonance (NMR) spectroscopy
  • 3D structure calculation
  • Actin binding assays

Related Experiment Videos

Main Results:

  • Single nebulin repeats bind to F-actin.
  • A single repeat is the minimal unit for nebulin-actin interaction.
  • Nebulin repeats exhibit transient helical conformation, stabilized by anionic detergents mimicking actin's negative charges.
  • A structural model of the F-actin-nebulin complex was proposed.

Conclusions:

  • Nebulin repeats are key functional units for actin binding.
  • Anionic charge interactions are critical for nebulin-actin complex formation.
  • The proposed model provides insights into thin filament regulation in skeletal muscle.