Fast local backbone dynamics of encapsulated ubiquitin.
J Am Chem Soc
; 128(30): 9580-1, 2006 Aug 02.
Article
en En
| MEDLINE
| ID: mdl-16866482
Backbone dynamics of ubiquitin confined within AOT reverse micelles have been evaluated based on analysis of 15N NMR relaxation data. Results indicate that upon encapsulation the protein experiences a slight overall increase in the value of the order parameter, S2, indicating a restriction in the average amplitude of fast local N-H bond vector motion. The largest increases in S2 upon encapsulation were concentrated in the region of beta-sheet 2 and, additionally, at the transitions of secondary structure motifs and loop regions. In addition, statistical analysis of the residue average ratio of the 15N longitudinal and transverse NMR relaxation time constants indicates that chemical exchange contributions to relaxation are consistent with previous aqueous studies. Earlier studies have demonstrated that native protein structure can be maintained in the encapsulated state. These results presented here establish that the dynamical behavior of encapsulated ubiquitin is likewise nativelike and adds important new observations regarding the enhancement of protein stability under confinement.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ubiquitina
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
J Am Chem Soc
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Estados Unidos