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

Chemical biology beyond binary codes.

S W Michnick1

  • 1Département de Biochimie, Université de Montréal, C.P. 6128, succursale centre-ville, H3C 3J7, Montreal, Que., Canada. stephen.michnick@umontreal.ca

Chemistry & Biology
|January 4, 2001
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

Quantification of dynamic protein complexes using Renilla luciferase fragment complementation applied to protein kinase A activities in vivo.

Proceedings of the National Academy of Sciences of the United States of America·2007
Same author

The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse.

Journal of molecular biology·2006
Same author

Massive sequence perturbation of the Raf ras binding domain reveals relationships between sequence conservation, secondary structure propensity, hydrophobic core organization and stability.

Journal of molecular biology·2006
Same author

Massive sequence perturbation of a small protein.

Proceedings of the National Academy of Sciences of the United States of America·2005
Same author

Gene function: getting specific, generally speaking.

Proceedings of the National Academy of Sciences of the United States of America·2002
Same author

Detection and visualization of protein interactions with protein fragment complementation assays.

Methods in molecular biology (Clifton, N.J.)·2002
Same journal

The Hedgehog Pathway Effector Smoothened Exhibits Signaling Competency in the Absence of Ciliary Accumulation.

Chemistry & biology·2017
Same journal

DIVERSE System: De Novo Creation of Peptide Tags for Non-enzymatic Covalent Labeling by In Vitro Evolution for Protein Imaging Inside Living Cells.

Chemistry & biology·2015
Same journal

Differential Regulation of Specific Sphingolipids in Colon Cancer Cells during Staurosporine-Induced Apoptosis.

Chemistry & biology·2015
Same journal

Synthetic Peptides as cGMP-Independent Activators of cGMP-Dependent Protein Kinase Iα.

Chemistry & biology·2015
Same journal

Unraveling the B. pseudomallei Heptokinase WcbL: From Structure to Drug Discovery.

Chemistry & biology·2015
Same journal

Vitamin C as Cancer Destroyer, Investigating Sulfhydration, and the Variability in CFTR Interactome.

Chemistry & biology·2015
See all related articles

Chemical dimerizers allow dynamic control over protein complex assembly and disassembly in living cells. This breakthrough enables the study of real biological pathways, moving beyond simple binary interactions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Cellular processes rely on complex macroassemblies of enzymes and nucleic acids.
  • Current methods for studying protein interactions are limited to observing binary complexes.
  • Understanding dynamic macromolecular assembly is crucial for deciphering biological pathways.

Purpose of the Study:

  • To introduce and highlight the utility of chemical dimerizers for studying dynamic protein complex formation.
  • To enable the investigation of 'real' biological pathways by controlling macromolecular assembly.
  • To overcome limitations of existing methods in observing complex biological interactions.

Main Methods:

  • Utilizing chemical dimerizers to dynamically induce or disrupt protein complex assembly in living cells.

Related Experiment Videos

  • Observing and analyzing the behavior of macromolecular assemblies under controlled conditions.
  • Comparing dimerizer-mediated assembly with traditional methods of studying protein interactions.

    • Main Results:

    • Demonstrated the ability of chemical dimerizers to control the formation and dissolution of protein complexes.
    • Provided a novel tool for observing dynamic changes in macromolecular assemblies.
    • Enabled the study of biological processes that were previously inaccessible due to methodological constraints.

    Conclusions:

    • Chemical dimerizers offer a powerful new approach to studying complex biological systems.
    • These tools facilitate a deeper understanding of dynamic macromolecular assembly and biochemical pathways.
    • The ability to manipulate protein complexes in real-time opens new avenues for biological research.