Effects upon the stability of Sfbglu caused by mutations surrounding central residues (2015)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- Subjects: ENZIMOLOGIA; MUTAÇÃO; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq)
- Publisher place: São Paulo
- Date published: 2015
- Source:
- Título: Abstracts Book
- Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - IUBMB
-
ABNT
SOUZA, V P e MARANA, Sandro Roberto. Effects upon the stability of Sfbglu caused by mutations surrounding central residues. 2015, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2015. . Acesso em: 10 jan. 2026. -
APA
Souza, V. P., & Marana, S. R. (2015). Effects upon the stability of Sfbglu caused by mutations surrounding central residues. In Abstracts Book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq). -
NLM
Souza VP, Marana SR. Effects upon the stability of Sfbglu caused by mutations surrounding central residues. Abstracts Book. 2015 ;[citado 2026 jan. 10 ] -
Vancouver
Souza VP, Marana SR. Effects upon the stability of Sfbglu caused by mutations surrounding central residues. Abstracts Book. 2015 ;[citado 2026 jan. 10 ] - The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase
- Single mutations outside the active site affect the substrate specificity in a ß-glycosidade
- Standardization of a method of In vitro evolution of beta-glycosidases
- Determinação do calor de reação para peroxiredoxinas
- Identification of domains in GH1 β-glucosidases based on the thermal and chemical stabilities
- Distribuicao intracelular de enzimas digestivas e caracterizacao das 'BETA'-glucosidases intestinais de abracris flavolineata
- Mutation of surface charged residues changes the affinity of lysozymes for bacterial walls
- 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
- Enzyme optimum temperature: constant or relative parameter?
- Data supporting the hypothesis that contact pathways modulate the substrate specificity of a β-glucosidase
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