Protein structure network and thermal stability (2016)
- Autor:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- Subjects: PROTEÍNAS; BIOINFORMÁTICA
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq)
- Publisher place: Natal
- Date published: 2016
- Source:
- Título do periódico: Abstracts
- Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology (SBBq)
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ABNT
MARANA, Sandro Roberto. Protein structure network and thermal stability. 2016, Anais.. Natal: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2016. . Acesso em: 30 abr. 2024. -
APA
Marana, S. R. (2016). Protein structure network and thermal stability. In Abstracts. Natal: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq). -
NLM
Marana SR. Protein structure network and thermal stability. Abstracts. 2016 ;[citado 2024 abr. 30 ] -
Vancouver
Marana SR. Protein structure network and thermal stability. Abstracts. 2016 ;[citado 2024 abr. 30 ] - 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
- Role of residue E190 in modulating aglycone specificity of a 'beta'-glycosidase from spodoptera frugiperda (SFBGLI50-AF 052729) of family 1
- In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol
- Data supporting the hypothesis that contact pathways modulate the substrate specificity of a β-glucosidase
- Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase
- Standardization of a method of In vitro evolution of beta-glycosidases
- The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase
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