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

[Structure-function organization of the angiotensin II molecule. II. Reverse structural problem]

T V Gogitidze, E M Popov

    Bioorganicheskaia Khimiia
    |July 1, 1993
    PubMed
    Summary

    Researchers modified the amino acid sequence of angiotensin II to create analogues with restricted conformations. These analogues exhibited distinct spatial structures and conformational energies compared to the native hormone, aiding in structure-activity relationship studies.

    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

    [Conformational analysis of cysteine-containing peptides and prospects of their application to 213Bi chelating in antitumor therapy].

    Bioorganicheskaia khimiia·2006
    Same author

    [Mechanism of aspartyl proteinase action. VII. Noncovalent complexes of HIV-1 aspartyl proteinase with substrate and substrate-like inhibitors].

    Bioorganicheskaia khimiia·2000
    Same author

    [Mechanism of action of aspartyl proteinases. VI. Nonvalent enzyme-inhibitory and enzyme-substrate complexes of the aspartyl proteinase rhizopus pepsin].

    Bioorganicheskaia khimiia·2000
    Same author

    [Mechanism of action of aspartic proteinases. V. Conformational characteristics of fragments of substrate-binding sites in rhizopuspepsin and HIV-1 proteinase].

    Bioorganicheskaia khimiia·1999
    Same author

    Protein folding as a nonlinear nonequilibrium thermodynamic process.

    Biochemistry and molecular biology international·1999
    Same author

    Mechanism of action of aspartic proteases.

    Advances in experimental medicine and biology·1998

    Area of Science:

    • Medicinal Chemistry
    • Structural Biology
    • Peptide Science

    Context:

    • Angiotensin II is a key peptide hormone regulating blood pressure.
    • Understanding its conformational dynamics is crucial for drug design.
    • Previous studies focused on the biological activity of angiotensin II analogues.

    Purpose:

    • To synthesize and analyze novel angiotensin II analogues.
    • To investigate the impact of amino acid modifications on conformational properties.
    • To compare the spatial structures and conformational energies of analogues with the native hormone.

    Summary:

    • Several modifications were made to the amino acid sequence of angiotensin II.
    • Conformational properties of the resulting analogues were restricted.

    Related Experiment Videos

  • Relative conformational energies were evaluated in low-energy conformations.
  • A comparative analysis of spatial structures was performed.

    • Impact:

    • Provides insights into structure-activity relationships of angiotensin II analogues.
    • Informs the design of peptide-based therapeutics with improved stability and specificity.
    • Contributes to the understanding of peptide hormone conformational flexibility.