期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 25, 期 3, 页码 343-350出版社
SPRINGER
DOI: 10.1007/s13361-013-0798-3
关键词
Electron transfer dissociation; Mass spectrometry; Surface mapping; Protein tetramer; Noncovalent complex; Top-down sequencing
资金
- Research Foundation - Flanders (FWO)
- Hercules Foundation - Flanders
- Flemish Institute for Technological Research (VITO)
Top-down approaches for the characterization of intact proteins and macromolecular complexes are becoming increasingly popular, since they potentially simplify and speed up the assignment process. Here we demonstrate how, on a commercially available Q-TWIMS-TOF instrument, we performed top-down ETD of the native form of tetrameric alcohol dehydrogenase. We achieved good sequence coverage throughout the first 81 N-terminal amino acids of ADH, with the exception of a loop located on the inside of the protein. This is in agreement with the exposed parts of the natively folded protein according to the crystal structure. Choosing the right precursor charge state and applying supplemental activation were found to be key to obtaining a high ETD fragmentation efficiency. Finally, we briefly discuss opportunities to further increase the performance of ETD based on our results.
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