Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase (2012)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- Subjects: AMINOÁCIDOS; BIOQUÍMICA
- 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
ZAPICO, Luis Felipe Martinho e MARANA, Sandro Roberto. Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase. 2012, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2012. . Acesso em: 31 dez. 2025. -
APA
Zapico, L. F. M., & Marana, S. R. (2012). Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq). -
NLM
Zapico LFM, Marana SR. Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase. Program and Index. 2012 ;[citado 2025 dez. 31 ] -
Vancouver
Zapico LFM, Marana SR. Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase. Program and Index. 2012 ;[citado 2025 dez. 31 ] - 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
- A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by beta-glucosidases
- Using the amino acid network to modulate the hydrolytic activity of beta-Glycosidases
- Protein thermal stability modulated by Hub residues
- 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
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