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

[Alpha-helix retention in prion proteins]

I B Kuznetsov1, P S Morozov, Iu G Matushkin

  • 1Institute of Cytology and Genetics, Russian Academy of Sciences, Novosibirsk, Russia.

Genetika
|May 20, 1998
PubMed
Summary

Prion diseases stem from altered prion proteins (PrP). Evolutionary analysis reveals substitutions that disrupt alpha-helices, promoting beta-structures, likely causing these neurodegenerative disorders.

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

[The influence of physiobalneotherapy on the hormonal status of men suffering from obesity].

Voprosy kurortologii, fizioterapii, i lechebnoi fizicheskoi kultury·2012
Same author

[Theories of biological evolution from the viewpoint of the modern systemic biology].

Genetika·2012
Same author

[Evolutionary trends in the prokaryotic community and prokaryotic community-phage systems].

Genetika·2012
Same author

[Correlation of codon biases and potential secondary structures with mRNA translation efficiency in unicellular organisms].

Molekuliarnaia biologiia·2008
Same author

[A generalized chemical-kinetic method for modeling gene networks].

Molekuliarnaia biologiia·2002
Same author

[On connection of a graph of a gene network with qualitative modes of function].

Molekuliarnaia biologiia·2002

Area of Science:

  • Biochemistry
  • Neuroscience
  • Evolutionary Biology

Background:

  • Prion diseases are neurodegenerative disorders.
  • They are caused by misfolded prion proteins (PrP).
  • Misfolding involves conformational changes, specifically the loss of alpha-helices.

Purpose of the Study:

  • To investigate the evolutionary changes in prion protein (PrP) sequences.
  • To understand the role of amino acid substitutions in PrP conformation.
  • To explore the link between PrP structural changes and prion disease pathogenesis.

Main Methods:

  • Phylogenetic analysis of 32 PrP sequences.
  • Analysis of evolutionary rates and substitution patterns.
  • Prediction of protein secondary structure changes using computational methods.

Main Results:

  • Prion proteins (PrP) show evolutionary rates indicating some sequence variability.
  • Conserved amino acid substitutions occurred in helical regions, maintaining physical/chemical properties.
  • Substitutions that disrupt alpha-helices were identified, particularly in human PrP sequences.

Conclusions:

  • Prion diseases are associated with conformational changes in PrP.
  • These changes involve the destruction of alpha-helices and the formation of beta-structures.
  • Evolutionary analysis supports the hypothesis that altered PrP conformation drives prion disease.

Related Experiment Videos