Effect of active site mutation on S and S binding energies in a beta-glycosidase (2005)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Programas e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
LIN, Fabio Leekuan Huang e MARANA, Sandro Roberto. Effect of active site mutation on S and S binding energies in a beta-glycosidase. 2005, Anais.. São Paulo: SBBq, 2005. . Acesso em: 12 nov. 2024. -
APA
Lin, F. L. H., & Marana, S. R. (2005). Effect of active site mutation on S and S binding energies in a beta-glycosidase. In Programas e Resumos. São Paulo: SBBq. -
NLM
Lin FLH, Marana SR. Effect of active site mutation on S and S binding energies in a beta-glycosidase. Programas e Resumos. 2005 ;[citado 2024 nov. 12 ] -
Vancouver
Lin FLH, Marana SR. Effect of active site mutation on S and S binding energies in a beta-glycosidase. Programas e Resumos. 2005 ;[citado 2024 nov. 12 ] - 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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