Data Processing in Bottom-Up Hydrogen Exchange Mass Spectrometry

Department of Biochemistry and Molecular Biology and the Southern Alberta Cancer Research Institute, University of Calgary, Calgary, Alberta, Canada 

Hydrogen Exchange Mass Spectrometry of Proteins Fundamentals, Methods, and Applications, First Edition. Edited by David D. Weis. 

If it were possible, we would measure deuteration at each and every backbone amide, as in an NMR experiment [11, 12]. It would be a deuteration value between 0 and 1, although still reflecting a population average deuteration. The bottom-up experiment provides such access through MS/MS-based peptide fragmentation (see Chapter 8), but we will begin a discussion of the deuteration measurement at the level of the intact peptide. Most applications never go beyond a peptide-level analysis, because the higher stmctural resolution measurements are somewhat difficult to measure for a whole protein [13] and because many structure/function questions can be addressed very adequately at the peptide level. 

The natural isotopic distribution of a peptide is dominated by the ratio, and it has a 

It is the goal of software to assign a peptide identity to the isotopic distribution, detect its expansion by the deuterium labeling experiment, and extract the key deuteration data. The important data are twofold an average deuteration value and a measure of the deuterium distribution of states. 

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Data Processing in Bottom-Up Hydrogen Exchange Mass Spectrometry... 

Data Processing in Bottom-Up Hydrogen Exchange Mass Spectrometry 47 Table 3.1 List of available software utilities for HX-MS analysis... 

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