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

Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.

Sunghyouk Park1, Michael S Caffrey, Michael E Johnson

  • 1Center for Pharmaceutical Biotechnology, University of Illinois, 900 S. Ashland, Chicago, IL 60607, USA.

The Journal of Biological Chemistry
|April 4, 2003
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

Vitamin B6 produced by gut microbiome regulates host behavioral phenotypes through dopaminergic metabolism.

Gut microbes·2026
Same author

NMR-Based Metabolic Profiling of Biobank Derived Blood Samples for the Identification of Liver Disease Biomarkers.

Biomolecules & therapeutics·2026
Same author

Pharmacomultiomics suggests new off-targets for targeted anti-cancer agents.

Journal of pharmaceutical analysis·2026
Same author

Altered acetate metabolism and signaling in IgA nephropathy: an integrated gut microbiome and glomerular spatial transcriptome analysis.

Frontiers in immunology·2026
Same author

Epigenetically-controlled CEBPB regulates kidney cancer tumorigenesis via GPD1L-mediated ether lipid synthesis.

Cell death & disease·2026
Same author

Live Metabolomics with NMR.

Analytical chemistry·2026

The solution NMR structure of erythroid alpha-spectrin reveals a flexible junction region. This flexibility may influence spectrin tetramer formation and associated physiological conditions.

Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular genetics

Background:

  • Spectrin forms the cytoskeleton in various cell types.
  • Alpha- and beta-spectrin subunits associate to form tetramers.
  • Understanding spectrin structure is crucial for cell stability and function.

Purpose of the Study:

  • To determine the solution NMR structure of the N-terminal domain of erythroid alpha-spectrin.
  • To investigate the structural and dynamic properties of spectrin domains involved in subunit association.
  • To elucidate the role of specific regions in modulating spectrin tetramer formation.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy
  • Paramagnetic spin labeling
  • Recombinant peptide expression and purification

Related Experiment Videos

Main Results:

  • The N-terminal 156 residues of erythroid alpha-spectrin were structurally characterized.
  • A flexible, disordered conformation was observed in the N-terminal 20 residues and the 7-residue junction region connecting helix C' to the triple helical bundle.
  • Helix C', involved in spectrin association, showed minimal interaction with the main structural domain.

Conclusions:

  • The flexible junction region may regulate alpha- and beta-spectrin association affinity.
  • These findings offer insights into the formation of different spectrin tetramer isoforms.
  • The study provides a basis for understanding spectrin-related physiological and pathological conditions.