The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme (2007)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- DOI: 10.1016/j.jsb.2007.07.008
- Subjects: LISOZIMAS; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Journal of Structural Biology
- ISSN: 1047-8477
- Volume/Número/Paginação/Ano: v. 160, n. 1, p. 83-92, 2007
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
CANÇADO, Fabiane Chaves et al. The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme. Journal of Structural Biology, v. 160, n. 1, p. 83-92, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2007.07.008. Acesso em: 18 abr. 2024. -
APA
Cançado, F. C., Valério, A. A., Marana, S. R., & Barbosa, J. A. R. G. (2007). The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme. Journal of Structural Biology, 160( 1), 83-92. doi:10.1016/j.jsb.2007.07.008 -
NLM
Cançado FC, Valério AA, Marana SR, Barbosa JARG. The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme [Internet]. Journal of Structural Biology. 2007 ; 160( 1): 83-92.[citado 2024 abr. 18 ] Available from: https://doi.org/10.1016/j.jsb.2007.07.008 -
Vancouver
Cançado FC, Valério AA, Marana SR, Barbosa JARG. The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme [Internet]. Journal of Structural Biology. 2007 ; 160( 1): 83-92.[citado 2024 abr. 18 ] Available from: https://doi.org/10.1016/j.jsb.2007.07.008 - 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
Informações sobre o DOI: 10.1016/j.jsb.2007.07.008 (Fonte: oaDOI API)
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