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

A model for prion protein dimerisation based on alpha-helical packing

J Warwicker1, P J Gane

  • 1Institute of Food Research, Reading Laboratory, United Kingdom. james.warwicker@bbsrc.ac.uk

Biochemical and Biophysical Research Communications
|September 24, 1996
PubMed
Summary

Researchers explored alpha-helical dimerisation in human prion protein (PrP) residues 109-122. A computational model suggests specific amino acid interactions may explain prion disease species barriers.

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

Polyunsaturated fatty acids inhibit Kv1.4 by interacting with positively charged extracellular pore residues.

American journal of physiology. Cell physiology·2016
Same author

Specific ion and buffer effects on protein-protein interactions of a monoclonal antibody.

Molecular pharmaceutics·2014
Same author

The role of electrostatics in protein-protein interactions of a monoclonal antibody.

Molecular pharmaceutics·2014
Same author

Freezing and folding behavior in simple off-lattice heteropolymers.

The Journal of chemical physics·2004
Same author

Biochemical and genetic evidence for a family of heterotrimeric G-proteins in Trichomonas vaginalis.

Molecular and biochemical parasitology·2003
Same author

A second eIF4E protein in Schizosaccharomyces pombe has distinct eIF4G-binding properties.

Nucleic acids research·2001

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • The human prion protein (PrP) cellular form (PrPc) contains a highly conserved alpha-helical region (residues 109-122).
  • Prion diseases involve the misfolded form (PrPSc) and are influenced by species-specific factors.

Purpose of the Study:

  • To computationally investigate the potential for alpha-helical dimerisation within PrP residues 109-122.
  • To model heterodimerisation between PrPc and PrPSc and explore its relation to species barrier mutations.

Main Methods:

  • Computational analysis of alpha-helical dimerisation potential for PrP residues 109-122.
  • Modeling of PrPc-PrPSc heterodimerisation based on identified homodimerisation frameworks.

Main Results:

Related Experiment Videos

  • A specific tight association conformation involving alanine, glycine, and valine residues consistently scored highest for burying non-polar surface area.
  • A model for PrPc-PrPSc heterodimerisation was developed, suggesting interaction specificities align with homodimer formation.

Conclusions:

  • The study identifies a likely structural basis for homodimerisation in a key PrP region.
  • This framework may also underlie the specificities of PrPc-PrPSc interactions, potentially explaining prion disease species barriers.