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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/16694

Title: ETD Allows for Native Surface Mapping of a 150 kDa Noncovalent Complex on a Commercial Q-TWIMS-TOF Instrument
Authors: Lermyte, Frederik
Konijnenberg, Albert
Williams, Jonathan P.
Brown, Jeffery M.
VALKENBORG, Dirk
Sobott, Frank
Issue Date: 2014
Citation: JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 25 (3), p. 343-350
Abstract: 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 topdown 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.
Notes: Sobott, F (reprint author), Univ Antwerp, Dept Chem, Biomol & Analyt Mass Spectrometry Grp, Groenenborgerlaan 171, B-2020 Antwerp, Belgium. Frank.Sobott@ua.ac.be
URI: http://hdl.handle.net/1942/16694
DOI: 10.1007/s13361-013-0798-3
ISI #: 000330831900006
ISSN: 1044-0305
Category: A1
Type: Journal Contribution
Validation: ecoom, 2015
Appears in Collections: Research publications

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