A Multidimensional Approach to Protein Characterization |
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Authors: | Robert J. Anderegg David S. Wagner R. Kevin Blackburn Gregory J. Opiteck James W. Jorgenson |
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Affiliation: | (1) Glaxo Wellcome, Inc., Research Triangle Park, North Carolina;(2) Department of Analytical Chemistry, Glaxo Wellcome Research Laboratories, Research Triangle Park, North Carolina, 27709;(3) Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina |
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Abstract: | When mass spectrometry (MS) is used to study protein primary structure, it is used in a static mode. That is, the information is derived from a single MS or MS-MS spectrum. Information about more complex protein structure or protein interactions can also be gained via MS. If a series of mass spectra is collected as something else in the experiment is changing, we increase the dimensionality of the MS data. For example, measuring mass spectra as a function of time after exposure of a protein to deuterated solvents can provide information about protein structure. Likewise, by measuring mass spectra of a protein as the concentration of a binding ligand is changed, one can infer the stoichiometry of the complex. Another important, but fundamentally different way of increasing the dimensionality of mass spectral data is by coupling the mass spectrometer to a one- or two-dimensional separation technique. |
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Keywords: | Mass spectrometry deuterium exchange two-dimensional separations secondary structure protein: ligand interaction |
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