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Probing Protein Structure and Folding in the Gas Phase by Electron Capture Dissociation

The established methods for the study of atom-detailed protein structure in the condensed phases, X-ray crystallography and nuclear magnetic resonance spectroscopy, have recently been complemented by new techniques by which nearly or fully desolvated protein structures are probed in gas-phase experi...

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Detalles Bibliográficos
Autores principales: Schennach, Moritz, Breuker, Kathrin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4475247/
https://www.ncbi.nlm.nih.gov/pubmed/25868904
http://dx.doi.org/10.1007/s13361-015-1088-z
Descripción
Sumario:The established methods for the study of atom-detailed protein structure in the condensed phases, X-ray crystallography and nuclear magnetic resonance spectroscopy, have recently been complemented by new techniques by which nearly or fully desolvated protein structures are probed in gas-phase experiments. Electron capture dissociation (ECD) is unique among these as it provides residue-specific, although indirect, structural information. In this Critical Insight article, we discuss the development of ECD for the structural probing of gaseous protein ions, its potential, and limitations. [Figure: see text]