DXMSMS Match Program for Automated Analysis of LC-MS/MS Data Obtained Using Isotopically Coded CID-Cleavable
Evgeniy V Petrotchenko1, Karl A T Makepeace1, Christoph H Borchers1,2
1University of Victoria - Genome British Columbia Proteomics Centre, University of Victoria, Victoria, Canada.
Current Protocols in Bioinformatics
|December 16, 2014
Summary
This study introduces DXMSMS Match, a program for automatically analyzing mass spectrometry data from isotopically coded cleavable cross-linkers. It aids in confidently identifying and assigning cross-links in protein complex studies.
Area of Science:
- Proteomics
- Biochemistry
- Analytical Chemistry
Background:
- Cross-linking combined with mass spectrometry is crucial for studying proteins and protein complexes.
- Isotopically coded cleavable cross-linking reagents enhance detection and assignment of cross-links.
- Automatic analysis of complex mass spectrometry data is needed.
Purpose of the Study:
- To describe the DXMSMS Match program for automatic analysis of LC-MS/MS data.
- To facilitate the study of proteins and protein complexes using isotopically coded cleavable cross-linkers.
- To improve the confidence and efficiency of cross-link assignment in mass spectrometry.
Main Methods:
- Development of the DXMSMS Match program for automated data analysis.
- Utilizing isotopically coded CID-cleavable cross-linkers.
- Verification of cross-link assignments using precursor mass and MS/MS spectra analysis, including fragments and cleavage products.
Main Results:
- The DXMSMS Match program provides automatic analysis of LC-MS/MS mass spectrometric data.
- The program verifies cross-link assignments through precursor mass and MS/MS spectral inspection.
- Nonprobabilistic scores and a visual interface are generated for validating mass spectral matches.
Conclusions:
- DXMSMS Match program facilitates confident detection and unambiguous assignment of cross-links.
- The software aids in the validation of mass spectral matches for cross-linked peptides.
- This tool enhances the study of protein and protein complex structures using mass spectrometry.
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