Fragmentation hydrogen exchange mass spectrometry: a review of methodology and applications.
Protein Expr Purif
; 84(1): 19-37, 2012 Jul.
Article
en En
| MEDLINE
| ID: mdl-22554819
ABSTRACT
The ability of proteins to function is intricately connected to proper folding and other environmental parameters. Methods and tools that are able to report back on structure and dynamics in native or otherwise desired environment are of utmost importance as they can be used to connect structure and function and provide us with deeper mechanistic understanding of the underlying principles involved. Besides, they might be useful in the verification of material quality and provide assurance of efficacy and soundness of experimental observations made with such materials. Hydrogen exchange mass spectrometry is one of those tools. It combines the universality of a "native" chemical labeling approach with an almost equally universally applicable detection scheme based on mass spectrometry that has already revolutionized proteomic research as a whole in the past. This review focuses on the concepts of the exchange method, advances in methodology that have made specifically the fragmentation hydrogen exchange mass spectrometry approach so successful, broadly surveys some of the application space, and highlights the most recent use in the area of biopharmaceutical development.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Espectrometría de Masas
/
Proteínas
/
Medición de Intercambio de Deuterio
Idioma:
En
Revista:
Protein Expr Purif
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2012
Tipo del documento:
Article
País de afiliación:
Estados Unidos