Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase (2012)
- Authors:
- USP affiliated authors: POLIKARPOV, IGOR - IFSC ; MARANA, SANDRO ROBERTO - IQ
- Unidades: IFSC; IQ
- Subjects: AMINOÁCIDOS; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq)
- Publisher place: São Paulo
- Date published: 2012
- Source:
- Título: Program and Index
- Conference titles: 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: 28 dez. 2025. -
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 2025 dez. 28 ] -
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 2025 dez. 28 ] - 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
- Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda
- 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
- 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
- Single mutations outside the active site affect the substrate specificity in a ß-glycosidade
- Structural and molecular basis for the acidic pH optimum of digestive lysozymes from housefly Musca domestica
- Characterization of '(β/α)'IND. 8'-barrel β-glycosidase
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