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

Polar zippers.

M F Perutz1, R Staden, L Moens

  • 1MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, UK.

Current Biology : CB
|May 1, 1993
PubMed
Summary
This summary is machine-generated.

Researchers discovered polar zippers in proteins, formed by beta strands, which may help assemble protein subunits. This finding expands our understanding of protein structure and function.

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

Diagnosis of deficiency of adenosine deaminase type 2 in adulthood.

Scandinavian journal of rheumatology·2021
Same author

Intrascrotal Collection in an Acute Pancreatitis: A Case Report and Review of the Literature.

Case reports in urology·2016
Same author

In situ Raman mapping of art objects.

Philosophical transactions. Series A, Mathematical, physical, and engineering sciences·2016
Same author

Effect of previous vaccination with pneumococcal conjugate vaccine on pneumococcal polysaccharide vaccine antibody responses.

Clinical and experimental immunology·2016
Same author

Evaluation of portable Raman spectroscopy and handheld X-ray fluorescence analysis (hXRF) for the direct analysis of glyptics.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy·2016
Same author

Assessment of a molecular diagnostic platform for integrated isolation and quantification of mRNA in whole blood.

European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology·2015
Same journal

Pitch selectivity in ferret auditory cortex.

Current biology : CB·2026
Same journal

A cell size-dependent competition between geometry and polarity governs nuclear and spindle positioning in early embryos.

Current biology : CB·2026
Same journal

Trophic cascades drive sustainability in the agricultural heritage rice-fish coculture system.

Current biology : CB·2026
Same journal

Tracking Satb2-positive retinal ganglion cells in zebrafish unveils developmental functional reorganization.

Current biology : CB·2026
Same journal

RhoGAP54D promotes cell size asymmetry and inhibits pulsatile myosin activity in Drosophila neural stem cells.

Current biology : CB·2026
Same journal

Increased rates of hybridization in swordtails are associated with water pollution.

Current biology : CB·2026
See all related articles

Area of Science:

  • Protein structure and biophysics
  • Molecular biology
  • Bioinformatics

Background:

  • Leucine zippers are common protein structures formed by alpha-helical coiled-coils.
  • Previous work suggested polar zippers in Ascaris haemoglobin subunits based on incomplete sequence data.
  • The carboxy-terminal peptides of Ascaris haemoglobin subunits were identified as a potential site for polar zipper formation.

Purpose of the Study:

  • To investigate the complete amino acid sequence of the carboxy-terminal peptide of Ascaris haemoglobin.
  • To determine the structural basis of subunit association in Ascaris haemoglobin.
  • To identify other proteins potentially forming polar zippers.

Main Methods:

  • Analysis of the complete cDNA-derived amino acid sequence of Ascaris haemoglobin.

Related Experiment Videos

  • Computer-based searches of protein databases for similar sequence repeats.
  • Structural modeling to predict the formation of antiparallel beta barrels and salt bridges.

    • Main Results:

    • The complete 24-residue carboxy-terminal peptide sequence of Ascaris haemoglobin is self-complementary, suggesting polar zipper formation.
    • These peptides can form an eight-stranded antiparallel beta barrel, with extensive salt bridges stabilizing subunit association.
    • Database searches revealed similar polar repeats in other proteins, including alternating arginine-aspartate, glutamine, and serine stretches.

    Conclusions:

    • Proteins can form polar zippers using beta strands, creating antiparallel pleated sheets stabilized by hydrogen bonds.
    • Polar zippers may be crucial for the stability of oligomeric proteins with limited surface complementarity.
    • These structures could also mediate the association of functionally related proteins.