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

[Neutral mutations and interference-stability of the genetic code].

M V Vol'kenshteĭn, N G Esipova

    Molekuliarnaia Biologiia
    |November 1, 1988
    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

    Role of structural water for prediction of cation binding sites in apoproteins.

    Journal of biomolecular structure & dynamics·2016
    Same author

    [Structural and Physicochemical Characteristics of Conformationally Stable alpha-Helical Oligopeptides].

    Biofizika·2015
    Same author

    [Disallowed conformations of polypeptide chain exemplified by the β-bend of the β-hairpin in the α-spectrin CH3-domain].

    Biofizika·2015
    Same author

    ["Co-phased blocks"--conservative regions of double-stranded DNA of transcriptional regulatory modules--are close in space due to phasing at nucleosome DNA super helix].

    Biofizika·2015
    Same author

    [On efficient in vitro purification of cell suspensions containing malignant cells].

    Biofizika·2015
    Same author

    [Classification of amino acids based on a comparative analysis of contacts in DNA-protein complexes and specific DNA-protein interactions].

    Biofizika·2014

    The neutral theory of evolution is compatible with genetic code safety, which is reflected in protein thermostability and conformational mobility. This study demonstrates no conflict between mutations affecting protein stability and neutral evolutionary processes.

    Area of Science:

    • Evolutionary Biology
    • Molecular Evolution
    • Biochemistry

    Context:

    • The neutral theory of molecular evolution posits that most evolutionary changes at the molecular level are driven by random drift of neutral mutations.
    • Protein thermostability is a crucial factor influencing protein function and is linked to conformational flexibility.
    • The genetic code's inherent safety mechanisms contribute to the robustness of protein synthesis.

    Purpose:

    • To explore the relationship between the neutral theory of evolution and the concept of genetic code safety.
    • To investigate whether protein thermostability and conformational mobility align with the principles of neutral evolution.
    • To determine if mutational changes in protein thermostability contradict the neutral theory.

    Summary:

    Related Experiment Videos

  • This research discusses the fundamental tenets of the neutral theory of evolution.
  • It demonstrates that the safety of the genetic code is intrinsically linked to the thermostability of proteins, specifically their conformational mobility.
  • The findings indicate no inherent contradiction between mutations altering protein thermostability and the predictions of the neutral theory.

    • Impact:

    • Provides evidence supporting the compatibility of neutral evolution with the functional constraints imposed by protein structure and stability.
    • Suggests that protein thermostability can be a neutral marker in evolutionary studies.
    • Deepens the understanding of molecular evolution by integrating genetic code properties with evolutionary mechanisms.