wrTopDownFrag: Internal Fragment Identification from Top-Down Mass Spectrometry
Top-Down mass spectrometry aims to identify entire proteins as well as their (post-translational) modifications or ions bound (eg Chen et al (2018) <doi:10.1021/acs.analchem.7b04747>).
The pattern of internal fragments (Haverland et al (2017) <doi:10.1007/s13361-017-1635-x>) may reveal important information about the original structure of the proteins studied
(Skinner et al (2018) <doi:10.1038/nchembio.2515> and Li et al (2018) <doi:10.1038/nchem.2908>).
However, the number of possible internal fragments gets huge with longer proteins and subsequent identification of internal fragments remains challenging,
in particular since the the accuracy of measurements with current mass spectrometers represents a limiting factor.
This package attempts to deal with the complexity of internal fragments and allows identification of terminal and internal fragments from deconvoluted mass-spectrometry data.
| Version: |
1.0.2 |
| Depends: |
R (≥ 3.1.0) |
| Imports: |
graphics, grDevices, stats, utils, wrMisc, wrProteo |
| Suggests: |
BiocParallel, boot, data.tree, fdrtool, knitr, limma, parallel, preprocessCore, RColorBrewer, rmarkdown, wrGraph |
| Published: |
2020-09-08 |
| Author: |
Wolfgang Raffelsberger [aut, cre] |
| Maintainer: |
Wolfgang Raffelsberger <w.raffelsberger at unistra.fr> |
| License: |
GPL-3 |
| NeedsCompilation: |
no |
| CRAN checks: |
wrTopDownFrag results |
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