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• W2080889700 endingPage "865" @default.
• W2080889700 startingPage "861" @default.
• W2080889700 abstract "Mass spectrometry (MS) has long been a tool of the analytical chemist. The advent of electrospray ionization (ESI) [1], together with the simultaneous development of matrix-assisted laser desorption ionization (MALDI) techniques [2], has now opened up this powerful technique to use by structural biologists. ESI MS and MALDI MS share common attributes such as their inherent sensitivity, ability to study mixtures and accuracy in determining the molecular weight of intact proteins [3–5]. The physical processes involved in obtaining mass spectra by these two methods are, however, very different; MALDI MS relies on a light-absorbing matrix and a laser pulse, to produce protein ions in the gas phase, and ESI MS produces multiply charged gas phase protein ions from solution. The ability of ESI MS to analyze intact protein samples directly from solution therefore provides new opportunities for studies of protein structure and function. In this article we draw attention to a group of applications in which ESI MS, combined with hydrogen-exchange labelling, is used to reveal information about the structure, folding and dynamics of proteins in solution." @default.
• W2080889700 created "2016-06-24" @default.
• W2080889700 creator A5003402066 @default.
• W2080889700 creator A5074934123 @default.
• W2080889700 date "1995-09-01" @default.
• W2080889700 modified "2023-09-25" @default.
• W2080889700 title "Weighing the evidence for structure: electrospray ionization mass spectrometry of proteins" @default.
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• W2080889700 doi "https://doi.org/10.1016/s0969-2126(01)00221-0" @default.
• W2080889700 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8535780" @default.
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