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

Calcium effects on calmodulin lysine reactivities.

D P Giedroc, D Puett, S K Sinha

    Archives of Biochemistry and Biophysics
    |January 1, 1987
    PubMed
    Summary

    Calcium binding to calmodulin causes differential changes in lysine reactivity. Lysine 75 shows a significant reactivity increase, while other lysines exhibit distinct binding patterns, revealing calmodulin

    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

    An analog-AI chip for energy-efficient speech recognition and transcription.

    Nature·2023
    Same author

    Association of Hashimoto's thyroiditis with thyroid cancer.

    Endocrine-related cancer·2014
    Same author

    Conversion of S-phenylsulfonylcysteine residues to mixed disulfides at pH 4.0: utility in protein thiol blocking and in protein-S-nitrosothiol detection.

    Organic & biomolecular chemistry·2014
    Same author

    Tissue inhibitor of metalloproteinases-1 protects human neurons from staurosporine and HIV-1-induced apoptosis: mechanisms and relevance to HIV-1-associated dementia.

    Cell death & disease·2012
    Same author

    A functional transmembrane complex: the luteinizing hormone receptor with bound ligand and G protein.

    Molecular and cellular endocrinology·2006
    Same author

    Giant cell arteritis of the female genital tract.

    Irish medical journal·2004

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Calmodulin (CaM) is a crucial calcium-binding protein involved in numerous cellular processes.
    • Understanding CaM's conformational changes upon calcium binding is key to elucidating its regulatory mechanisms.
    • Lysine residues are important for protein structure and function, and their reactivity can indicate microenvironmental changes.

    Purpose of the Study:

    • To investigate the differential reactivities of individual lysine residues in porcine testicular calmodulin.
    • To correlate these reactivity changes with varying calcium (Ca2+) to calmodulin molar ratios.
    • To elucidate the Ca2+-binding model of calmodulin based on lysine modification patterns.

    Main Methods:

    • Trace labeling of porcine testicular calmodulin using high specific activity [3H]acetic anhydride.
    • Quantification of lysine reactivity at different Ca2+:calmodulin molar ratios (0 to 5:1).
    • Analysis of reactivity changes normalized to maximum change to classify lysine residue behavior.

    Main Results:

    • Six of seven lysines showed modest reactivity increases (1.5-3.0-fold) with increasing Ca2+.
    • Lysine 75 exhibited a pronounced reactivity enhancement (>20-fold), indicating significant conformational change.
    • Lysines in the C-terminal domains (94, 148) responded early (2:1 ratio), while N-terminal lysines (13, 21, 30) and Lys 75 responded later (2-5:1 ratio).

    Conclusions:

    • Ca2+ binding likely initiates in the C-terminal domains, causing minor perturbations in the N-terminal domains.
    • Subsequent Ca2+ binding to the N-terminal domains induces larger conformational shifts, particularly affecting Lys 75 in the central helix.
    • Lysine 94 in apocalmodulin is perturbed by EGTA, suggesting potential interaction sites for chelating agents.

    Related Experiment Videos