Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure.
Appl Environ Microbiol
; 72(4): 3021-5, 2006 Apr.
Article
em En
| MEDLINE
| ID: mdl-16598011
ABSTRACT
The three-dimensional (3D) structure of the hyperthermophilic esterase EstE1 was constructed by homology modeling using Archaeoglobus fulgidus esterase as a reference, and the thermostability-structure relationship was analyzed. Our results verified the predicted 3D structure of EstE1 and identified the ion pair networks and hydrophobic interactions that are critical determinants for the thermostability of EstE1.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Archaeoglobus fulgidus
/
Esterases
/
Temperatura Alta
Tipo de estudo:
Prognostic_studies
/
Risk_factors_studies
Idioma:
En
Revista:
Appl Environ Microbiol
Ano de publicação:
2006
Tipo de documento:
Article