Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase (2012)
- Autores:
- Autores USP: POLIKARPOV, IGOR - IFSC ; MARANA, SANDRO ROBERTO - IQ
- Unidades: IFSC; IQ
- Assuntos: AMINOÁCIDOS; PROTEÍNAS
- Idioma: Inglês
- Imprenta:
- Editora: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq)
- Local: São Paulo
- Data de publicação: 2012
- Fonte:
- Título do periódico: Program and Index
- Nome do evento: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society (SBBq)
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ABNT
TAMAKI, Fabio Kendi et al. Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase. 2012, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2012. . Acesso em: 19 abr. 2024. -
APA
Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2012). Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq). -
NLM
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase. Program and Index. 2012 ;[citado 2024 abr. 19 ] -
Vancouver
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase. Program and Index. 2012 ;[citado 2024 abr. 19 ] - Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability
- Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda
- Functional sectors involved in thermal stability and activity in beta-glucosidases
- Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda
- Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases
- Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans
- Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis
- 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
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