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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/11468

Monitoring and modeling of protein processes using mass spectrometry, circular dichroism, and multivariate curve resolution methods

AutorNavea, Susana; Tauler, Romà; Juan, Anna de
Palabras claveProtein processes
Protein modeling
Mass Spectrometry
Circular dichroism
Curve resolution methods
Integration techniques
Fecha de publicación16-jun-2006
EditorAmerican Chemical Society
CitaciónAnalytical Chemistry 78(14): 4768-4778 (2006)
ResumenMass spectrometry has recently become one of the major analytical tools to study biomolecular structure and function. Ionization techniques, such as electrospray ionization (ESI), desorb biomolecules from solution to the gas phase keeping practically intact their natural structure. ESI applied to a protein solution produces a mixture of multiply charged ions, the ion charge distribution of which depends on the oligomeric form (mass) and on the protein surface exposed (amount of accommodated charges) of the related protein conformation. ESI-MS provides an efficient way to monitor protein processes; however, the ionic contributions of the different protein conformations involved usually overlap, and the use of chemometric tools is necessary to unravel the information related to the pure conformations that the biomolecule adopts along the process. Multivariate curve resolution-alternating least squares applied to MS-monitored protein processes provides the concentration profiles associated with the different protein conformations occurring during the process and the related pure mass spectra. The concentration profiles, in this context, the ionic contributions, describe the process mechanism and the structural information derived from the pure mass spectra characterizes the involved conformations. Mass spectra can be expressed schematically through percentages of base peak intensity. This chemical transformation compresses significantly the raw spectra and allows for an easier application of natural MS-related constraints, such as the presence of only one maximum, i.e., the base peak of a particular conformation, into the resolution of the pure signals. The combination of mass spectrometry and multivariate curve resolution methods is used to elucidate the mechanism of the pH-induced conformation changes of the bovine β-lactoglobulin. As a final step, MS data are fused with circular dichroism data and are simultaneously analyzed to ensure and confirm that all the previously detected MS conformations really exist in solution and are an artifact of neither the ionization process nor their chemometric resolution.
Descripción11 pages, 10 figures.-- PMID: 16841894 [PubMed].-- Printed version published Jul 15, 2006.
Versión del editorhttp://dx.doi.org/10.1021/ac052257r
ISSN0003-2700 (Print)
1520-6882 (Online)
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