ISSN:
1573-4943
Keywords:
Mass spectrometry
;
deuterium exchange
;
two-dimensional separations
;
secondary structure
;
protein: ligand interaction
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1026373830301
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