Collisional and Coulombic unfolding of gas-phase proteins: high correlation to their domain structures in solution.
Angew Chem Int Ed Engl
; 53(35): 9209-12, 2014 Aug 25.
Article
em En
| MEDLINE
| ID: mdl-24990104
ABSTRACT
The three-dimensional structures adopted by proteins are predicated by their many biological functions. Mass spectrometry has played a rapidly expanding role in protein structure discovery, enabling the generation of models for both proteins and their higher-order assemblies. While important coursed-grained insights have been generated, relatively few examples exist where mass spectrometry has been successfully applied to the characterization of protein tertiary structure. Here, we demonstrate that gas-phase unfolding can be used to determine the number of autonomously folded domains within monomeric proteins. Our ion mobility-mass spectrometry data highlight a strong, positive correlation between the number of protein unfolding transitions observed in the gas phase and the number of known domains within a group of sixteen proteins ranging from 8-78â
kDa. This correlation and its potential uses for structural biology is discussed.
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Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Desdobramento de Proteína
/
Gases
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Ano de publicação:
2014
Tipo de documento:
Article