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

Caged phosphoproteins.

Deborah M Rothman1, E James Petersson, M Eugenio Vázquez

  • 1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.

Journal of the American Chemical Society
|January 20, 2005
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

Stabilized thioamide peptide agonists of the neuropeptide Y type 2 receptor for targeted cancer imaging.

RSC chemical biology·2026
Same author

Glycoconjugate diversification in <i>Campylobacter concisus</i> is determined by two glycosyltransferases.

bioRxiv : the preprint server for biology·2026
Same author

Targeted Mutations Activate Allosteric Modulation of α5-Containing Nicotinic Acetylcholine Receptors.

ACS chemical neuroscience·2026
Same author

Determination of α-Synuclein Protein Interactions by μMap Photoproximity Labeling.

Journal of the American Chemical Society·2026
Same author

Detergent Exchange from Lipid Nanoparticles into Detergent Micelles Unlocks a Tool for Biochemical and Kinetic Characterization of Membrane Proteins.

Biochemistry·2026
Same author

Machine learning prediction of multiple distinct high-affinity chemotypes for α-synuclein fibrils.

Chemical communications (Cambridge, England)·2026
Same journal

Proton-Gated Torsional Spring for Molecular Energy Storage.

Journal of the American Chemical Society·2026
Same journal

Topologically Programmed Dual-Channel Covalent Organic Frameworks Decouple Gas and Ion Fluxes for Acidic CO<sub>2</sub> Electroreduction.

Journal of the American Chemical Society·2026
Same journal

Plasmonic Re-Excitation Enables Superoxide-Mediated Ethane Conversion to Acetic Acid under Visible Light.

Journal of the American Chemical Society·2026
Same journal

Photocatalytic Controlled Halodefluorination of Perfluoroalkyl Compounds Using <i>N</i>-Arylphenothiazines.

Journal of the American Chemical Society·2026
Same journal

Photoinduced Disproportionation Enables Oxidative Addition of Aryl Iodides at a Gallium(I) Center.

Journal of the American Chemical Society·2026
Same journal

Biocatalytic C3 β-<i>O</i>-Glycosylation of Triterpenes and Sterols to Synthesize Natural and Unnatural Saponins.

Journal of the American Chemical Society·2026
See all related articles

Researchers synthesized caged phosphoproteins using novel chemical and biological methods. This technique allows for the precise insertion of modified amino acids into proteins for advanced biological studies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Synthesis

Background:

  • Phosphoproteins play crucial roles in cellular signaling pathways.
  • Controlling protein phosphorylation sites is essential for studying protein function.
  • Existing methods for site-specific phosphorylation are limited.

Purpose of the Study:

  • To develop a method for the chemical and biological synthesis of caged phosphoproteins.
  • To enable the site-specific incorporation of photocleavable phosphoamino acid analogues into proteins.
  • To demonstrate the utility of this method in studying key signaling proteins.

Main Methods:

  • Synthesis of phosphoamino acid analogues (serine, threonine, tyrosine) with a photocleavable o-nitrophenylethyl group.
  • Development of a novel phosphitylating agent for amino acyl tRNA adduct formation.

Related Experiment Videos

  • Utilizing in vitro nonsense codon suppression methodology for protein synthesis.
  • Incorporation of modified amino acids into the nicotinic acetylcholine receptor (nAChR) and vasodilator-stimulated phosphoprotein (VASP).

    • Main Results:

    • Successful chemical and biological synthesis of caged phosphoamino acid analogues.
    • Demonstrated the feasibility of incorporating bulky, charged amino acids into proteins via in vitro translation.
    • Confirmed the successful incorporation into the alpha-subunit of nAChR and VASP.
    • Established a novel method for site-specific protein phosphorylation.

    Conclusions:

    • The in vitro nonsense codon suppression methodology enables the synthesis of caged phosphoproteins.
    • This technique allows for the precise introduction of modified phosphoamino acids into target proteins.
    • The developed method provides a powerful tool for investigating the function of phosphoproteins in biological systems.