Return
Isotope-Coded Labeling for Accelerated Protein Interaction Profiling Using MS
DOI:10.1021/acs.analchem.5b01410.png)
Abstract
En 中文
Protein interaction surface mapping using MS is widely applied but comparatively resource-intensive. Here, a workflow adaptation for use of isotope-coded tandem mass tags for the purpose is reported. The key benefit of improved throughput derived from sample acquisition multiplexing and automated analysis is shown to be maintained in the new application. Mapping of the epitopes of two monoclonal antibodies on their respective targets serves to illustrate the novel approach. We conclude that the approach enables mapping of interactions by MS at significantly larger scales than hereto possible.
Keywords:
EXCHANGE-MASS-SPECTROMETRY
CHEMICAL CROSS-LINKING
FAST PHOTOCHEMICAL OXIDATION
HYDROGEN/DEUTERIUM EXCHANGE
HYDROGEN-EXCHANGE
STRUCTURAL PROTEOMICS
SURFACE DISPLAY
RADICAL PROBE
COMPLEX
DIETHYLPYROCARBONATE
Journal
IF:
6.7
Papers:
4.7W
Citations:
15.9W
Organization
Cited Papers
Quantitative profiling of serum samples using TMT protein labelling, fractionation and LC-MS/MS
METHODS
IF4.3
Tandem mass tags:: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
ANALYTICAL CHEMISTRY
IF6.7
Chemical Cross-Linking and Mass Spectrometry As a Low-Resolution Protein Structure Determination Technique
ANALYTICAL CHEMISTRY
IF6.7
Study of the ribonuclease-S-protein-peptide complex using a radical probe and electrospray ionization mass spectrometry
ANALYTICAL CHEMISTRY
IF6.7

