Functional sectors involved in thermal stability and activity in beta-glucosidases (2014)
- Authors:
- USP affiliated authors: POLIKARPOV, IGOR - IFSC ; MARANA, SANDRO ROBERTO - IQ
- Unidades: IFSC; IQ
- DOI: 10.1002/pro.2504
- Subjects: ENZIMAS; TEMPERATURA
- Language: Inglês
- Imprenta:
- Publisher: Wiley-Blackwell
- Publisher place: Hoboken
- Date published: 2014
- Source:
- Título do periódico: Protein Science
- ISSN: 0961-8368
- Volume/Número/Paginação/Ano: v. 23, n. S1, p. 190-191, abstr. POST 03-279, July 2014
- Conference titles: Annual Symposium of the Protein Society
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: bronze
-
ABNT
TAMAKI, Fabio K. et al. Functional sectors involved in thermal stability and activity in beta-glucosidases. Protein Science. Hoboken: Wiley-Blackwell. Disponível em: https://doi.org/10.1002/pro.2504. Acesso em: 23 abr. 2024. , 2014 -
APA
Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2014). Functional sectors involved in thermal stability and activity in beta-glucosidases. Protein Science. Hoboken: Wiley-Blackwell. doi:10.1002/pro.2504 -
NLM
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Functional sectors involved in thermal stability and activity in beta-glucosidases [Internet]. Protein Science. 2014 ; 23( S1): 190-191.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1002/pro.2504 -
Vancouver
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Functional sectors involved in thermal stability and activity in beta-glucosidases [Internet]. Protein Science. 2014 ; 23( S1): 190-191.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1002/pro.2504 - Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability
- 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
- Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase
- Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases
- Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans
- Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis
- 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
Informações sobre o DOI: 10.1002/pro.2504 (Fonte: oaDOI API)
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