.png){kind=icon}
返回
Isotope-Coded Labeling for Accelerated Protein Interaction Profiling Using MS
.png){kind=icon}
OA
AI
DOI：10.1021/acs.analchem.5b01410.png)
.png){kind=icon}
.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
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.
Keyword:
EXCHANGE-MASS-SPECTROMETRY
CHEMICAL CROSS-LINKING
FAST PHOTOCHEMICAL OXIDATION
HYDROGEN/DEUTERIUM EXCHANGE
HYDROGEN-EXCHANGE
STRUCTURAL PROTEOMICS
SURFACE DISPLAY
RADICAL PROBE
COMPLEX
DIETHYLPYROCARBONATE
AI总结
对已上传原文的论文进行重点信息的提取，主要内容包括：简要概述、研究摘要、背景介绍、关键亮点、图文解析、展望与总结。
期刊
IF:
6.7
论文数:
4.7W
被引数:
15.9W
机构
引用论文
Quantitative profiling of serum samples using TMT protein labelling, fractionation and LC-MS/MS.png)
METHODS
METHODSIF4.3
PREAI
分享收藏Tandem mass tags:: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MSANALYTICAL CHEMISTRY
ANALYTICAL CHEMISTRYIF6.7
PREAI
分享收藏Chemical Cross-Linking and Mass Spectrometry As a Low-Resolution Protein Structure Determination TechniqueANALYTICAL CHEMISTRY
ANALYTICAL CHEMISTRYIF6.7
PREAI
分享收藏Study of the ribonuclease-S-protein-peptide complex using a radical probe and electrospray ionization mass spectrometryANALYTICAL CHEMISTRY
ANALYTICAL CHEMISTRYIF6.7
PREAI
分享收藏
查看更多内容