Ion mobility mass spectrometry of proteins in a modified commercial mass spectrometer
UNSPECIFIED. (2004) Ion mobility mass spectrometry of proteins in a modified commercial mass spectrometer. INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 236 (1-3). pp. 55-63. ISSN 1387-3806Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/j.ijms.2004.05.008
Ion mobility has emerged as an important technique for determining biopolymer conformations in solvent free environments. These experiments have been nearly exclusively performed on home built systems. In this paper we describe modifications to a commercial high performance mass spectrometer, the Waters UK "Uhima" Q-Tof, that allows high sensitivity measurement of peptide and protein cross sections. Arrival time distributions are obtained for a series of peptides (bradykinin, LHRH, substance P, bombesin) and proteins (bovine and equine cytochrome c, myoglobin, alpha-lactalbumin) with good agreement found with literature cross sections where available. In complex ATD's, mass spectra can be obtained for each feature confirming assignments. The increased sensitivity of the commercial instrument is retained along with the convenience of the data system, crucial features for analysis of protein misfolding systems. (C) 2004 Elsevier B.V. All rights reserved.
|Item Type:||Journal Article|
|Subjects:||Q Science > QC Physics|
|Journal or Publication Title:||INTERNATIONAL JOURNAL OF MASS SPECTROMETRY|
|Publisher:||ELSEVIER SCIENCE BV|
|Official Date:||August 2004|
|Number of Pages:||9|
|Page Range:||pp. 55-63|
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