Deuteration distribution estimation with improved sequence coverage for HX/MS experiments
Time-resolved hydrogen exchange (HX) followed by mass spectrometry (MS) is a key technology for studying protein structure, dynamics and interactions. HX experiments deliver a time-dependent distribution of deuteration levels of peptide sequences of the protein of interest. The robust and complete e...
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| Main Authors: | , , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
May 3, 2010
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| In: |
Bioinformatics
Year: 2010, Volume: 26, Issue: 12, Pages: 1535-1541 |
| ISSN: | 1367-4811 |
| DOI: | 10.1093/bioinformatics/btq165 |
| Online Access: | Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1093/bioinformatics/btq165 Verlag, lizenzpflichtig, Volltext: https://academic.oup.com/bioinformatics/article/26/12/1535/281316?login=true |
| Author Notes: | Xinghua Lou, Marc Kirchner, Bernhard Y. Renard, Ullrich Köthe, Sebastian Boppel, Christian Graf, Chung-Tien Lee, Judith A.J. Steen, Hanno Steen, Matthias P. Mayer and Fred A. Hamprecht |
MARC
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| 520 | |a Time-resolved hydrogen exchange (HX) followed by mass spectrometry (MS) is a key technology for studying protein structure, dynamics and interactions. HX experiments deliver a time-dependent distribution of deuteration levels of peptide sequences of the protein of interest. The robust and complete estimation of this distribution for as many peptide fragments as possible is instrumental to understanding dynamic protein-level HX behavior. Currently, this data interpretation step still is a bottleneck in the overall HX/MS workflow. | ||
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