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

Temperature dependent conformational changes in calmodulin.

P Gangola, H C Pant

    Biochemical and Biophysical Research Communications
    |February 28, 1983
    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

    Notch and Cdk5 in Zebrafish Mindbomb Mutant: Co-regulation or Coincidence?

    Folia biologica·2018
    Same author

    Localization of Myelin Proteins in the Developing Shark Spinal Cord.

    The Biological bulletin·2018
    Same author

    Computational study of the inhibitory mechanism of the kinase CDK5 hyperactivity by peptide p5 and derivation of a pharmacophore.

    Journal of computer-aided molecular design·2016
    Same author

    Acute and chronic stress differentially regulate cyclin-dependent kinase 5 in mouse brain: implications to glucocorticoid actions and major depression.

    Translational psychiatry·2015
    Same author

    Role of protein phosphatase 2A in Alzheimer's disease.

    Current Alzheimer research·2011
    Same author

    Structural and dynamic determinants of ligand binding and regulation of cyclin-dependent kinase 5 by pathological activator p25 and inhibitory peptide CIP.

    Journal of molecular biology·2010

    Calcium-bound calmodulin undergoes a reversible conformational change between 22-28°C. This transition temperature is influenced by calcium ion concentration, affecting calmodulin

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Structural Biology

    Background:

    • Calmodulin (CaM) is a crucial calcium-binding protein involved in numerous cellular signaling pathways.
    • Understanding CaM's conformational dynamics is essential for elucidating its regulatory mechanisms.

    Purpose of the Study:

    • To investigate the temperature-dependent conformational changes of calcium-bound calmodulin.
    • To determine the effect of calcium ion concentration on calmodulin's transition temperature.

    Main Methods:

    • Spectroscopic techniques were employed to monitor calmodulin's structural changes.
    • Varying concentrations of calcium ions were used to study their influence on CaM conformation.

    Main Results:

    Related Experiment Videos

  • Calcium-bound calmodulin exhibits a reversible conformational transition within the 22-28°C range.
  • The transition temperature is directly correlated with calcium ion concentration, occurring at 28°C for fully saturated CaM and 22°C for partially saturated states.
  • The order of calcium ion binding to the four sites differs between the two temperature-dependent conformers.
  • Conclusions:

    • Calmodulin's conformational flexibility is modulated by calcium ion stoichiometry.
    • These findings provide insights into the dynamic nature of calmodulin and its response to varying intracellular calcium levels.