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

Local interactions as a structure determinant for protein molecules: II

W R Krigbaum, A Komoriya

    Biochimica Et Biophysica Acta
    |January 25, 1979
    PubMed
    Summary

    Van der Waals interactions between protein sidechains are crucial for native protein structure. These interactions drive nonpolar sidechains to cluster and similar polarities to associate, influencing overall protein folding.

    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

    Use of enzymes in peptide synthesis.

    Applied biochemistry and biotechnology·2013
    Same author

    Characterization of fluorescence quenching in bifluorophoric protease substrates.

    Biophysical chemistry·2006
    Same author

    Caspase 8 activity in membrane blebs after anti-Fas ligation.

    Journal of immunology (Baltimore, Md. : 1950)·2001
    Same author

    Assessment of caspase activities in intact apoptotic thymocytes using cell-permeable fluorogenic caspase substrates.

    The Journal of experimental medicine·2000
    Same author

    Tumor cell recognition by lymphocytes: is the MHC always essential?

    Critical reviews in immunology·1998
    Same author

    Design of profluorescent protease substrates guided by exciton theory.

    Methods in enzymology·1997

    Area of Science:

    • Biophysics
    • Computational Biology
    • Protein Science

    Background:

    • Van der Waals interactions are fundamental forces in molecular interactions.
    • Protein structure is determined by various forces, including sidechain interactions.
    • Previous observations suggest specific patterns in protein sidechain distribution and pairing.

    Purpose of the Study:

    • To investigate the impact of Van der Waals interactions on protein structure.
    • To model how sidechain interactions influence protein folding and native states.

    Main Methods:

    • Analysis of radial distribution of polarity in known protein structures.
    • Examination of nonpolar sidechain clustering.
    • Statistical analysis of nearest-neighbor sidechain pairs.
    • Development and application of three simplified protein models: sheath-core, chain-connected modification, and concentric spherical phases.

    Main Results:

    • Observed increase in polarity from protein core to periphery.
    • Identified clustering of nonpolar sidechains.
    • Demonstrated non-random, polarity-driven associations between nearest-neighbor sidechains.
    • Results from simplified models support the significant role of Van der Waals forces.

    Conclusions:

    • Van der Waals interactions between protein sidechains play a critical role in determining native protein structure.
    • Sidechain interactions, driven by polarity, contribute to the hierarchical organization of protein molecules.
    • Simplified modeling approaches can effectively elucidate fundamental principles of protein folding.

    Related Experiment Videos