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

Probing protein tertiary structure with amidination.

Dariusz J Janecki1, Richard L Beardsley, James P Reilly

  • 1Department of Chemistry, Indiana University, Bloomington, 47405, USA.

Analytical Chemistry
|November 16, 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

Locating Polyubiquitin Receptors on the 19S Regulatory Proteasome of <i>S. cerevisiae</i> by Cross-Linking Mass Spectrometry.

Journal of the American Society for Mass Spectrometry·2025
Same author

Discovery and Characterization of Unusual O-Linked Glycosylation of IgG4 Antibody Using LC-MS.

Rapid communications in mass spectrometry : RCM·2024
Same author

MEMS and ECM Sensor Technologies for Cardiorespiratory Sound Monitoring-A Comprehensive Review.

Sensors (Basel, Switzerland)·2024
Same author

Patient-centric Comparability Assessment of Biopharmaceuticals.

Journal of pharmaceutical sciences·2024
Same author

Integrated summary of immunogenicity of polatuzumab vedotin in patients with relapsed or refractory B-cell non-Hodgkin's lymphoma.

Frontiers in immunology·2023
Same author

Tracking auditory mismatch negativity responses during full conscious state and coma.

Frontiers in neurology·2023
Same journal

Heterojunction Gate-Empowered OPECT Aptasensing: A Valid Protocol for Realizing High Current Gain at Low Electron Donor Dependency.

Analytical chemistry·2026
Same journal

Development of a Tapping-Mode Scanning Probe Electrospray Ionization Platform for High-Sensitivity and Long-Term Stability in Single-Cell Mass Spectrometry Imaging of Tissue.

Analytical chemistry·2026
Same journal

A Solid-State Near-Infrared Fluorescent Probe by a Synergistic Extended Conjugated System for Detecting Cys with Long-Term Imaging in Orthotopic Bladder Cancer.

Analytical chemistry·2026
Same journal

Air-Based Porous Array Dielectric Barrier Discharge Ionization Source for Explosive Trace Detection.

Analytical chemistry·2026
Same journal

PSAQ<sup>+1</sup>: Absolute Protein Quantification Using a <sup>13</sup>C<sub>1</sub>-Labeled Protein Standard, Coisolation of Peptide Pairs and LC-PRM.

Analytical chemistry·2026
Same journal

Heterojunction-Enhanced Interfacial Evanescent-Tunable Fiber Optic Probe for Amplification-free CRISPR/Cas12a-Based Rapid and Ultrasensitive Detection of MPXV.

Analytical chemistry·2026
See all related articles

Amidination, a chemical modification technique, rapidly maps solvent-accessible lysine residues in proteins. This method aids in understanding protein structure and accessibility using mass spectrometry.

Area of Science:

  • Proteomics
  • Chemical Biology
  • Structural Biology

Background:

  • Amidination is a chemical derivatization method used in peptide mass spectrometry.
  • Understanding protein solvent accessibility is crucial for studying protein structure and function.

Purpose of the Study:

  • To apply amidination for covalently modifying lysine residues in standard proteins.
  • To rapidly elucidate solvent-accessible regions of folded proteins using mass spectrometry.

Main Methods:

  • Chemical derivatization using amidination.
  • Protein and peptide mass spectrometry analysis.
  • Identification of modified and unmodified lysine sites.

Main Results:

  • Amidination successfully modified accessible lysine residues in standard proteins.

Related Experiment Videos

  • Mass spectrometry identified specific sites of reaction, distinguishing accessible from inaccessible lysines.
  • The method proved rapid for mapping solvent accessibility.

    • Conclusions:

    • Amidination is an effective and rapid technique for mapping solvent-accessible regions in folded proteins.
    • This approach provides insights into protein surface accessibility and structural dynamics.
    • The study highlights the utility of chemical modification coupled with mass spectrometry in structural biology.