Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda (2012)
- Autores:
- Autores USP: POLIKARPOV, IGOR - IFSC ; MARANA, SANDRO ROBERTO - IQ
- Unidades: IFSC; IQ
- Assuntos: ENZIMAS (ESTUDO); PROTEÍNAS; AMINOÁCIDOS
- Idioma: Inglês
- Imprenta:
- Editora: Sociedad Española de Bioquímica y Biología Molecular - SEBBM
- Local: Madri
- Data de publicação: 2012
- Fonte:
- Título: Program
- Volume/Número/Paginação/Ano: Madri : Sociedad Española de Bioquímica y Biología Molecular - SEBBM, 2012
- Nome do evento: Congress of the International Union of Biochemistry and Molecular Biology - IUBMB
-
ABNT
TAMAKI, Fabio K. et al. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. 2012, Anais.. Madri: Sociedad Española de Bioquímica y Biología Molecular - SEBBM, 2012. . Acesso em: 01 out. 2024. -
APA
Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2012). Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. In Program. Madri: Sociedad Española de Bioquímica y Biología Molecular - SEBBM. -
NLM
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. Program. 2012 ;[citado 2024 out. 01 ] -
Vancouver
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. Program. 2012 ;[citado 2024 out. 01 ] - Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability
- Functional sectors involved in thermal stability and activity in beta-glucosidases
- Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases
- Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase
- Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis
- Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans
- Optimum temperature may be a misleading parameter in enzyme characterization and application
- Enzyme optimum temperature: constant or relative parameter?
- Role of the triad N46, S106 and T107 and the surface charges in the determination of the acidic pH optimum of digestive lysozymes from Musca domestica
- Additivity of mutational effects on the catalytic activity of a 'beta'glycosidase
Como citar
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas