Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell division protein ZipA.
Chem Commun (Camb)
; 52(39): 6541-4, 2016 May 05.
Article
em En
| MEDLINE
| ID: mdl-27109863
ABSTRACT
The sensitivity of QCM-D to molecular hydrodynamic properties is applied in this work to study conformational changes of the intrinsically disordered protein ZipA. Acoustic measurements can clearly follow ZipA's unstructured domain expansion and contraction with salt content and be correlated with changes in the hydrodynamic radius of 1.8 nm or less.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Transporte
/
Proteínas de Ciclo Celular
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Proteínas de Escherichia coli
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Proteínas Intrinsicamente Desordenadas
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article