Thermal denaturation of the Na,K-ATPase solubilized and incorporated in DPPC:DPPE-liposomes (2005)
- Authors:
- USP affiliated authors: WARD, RICHARD JOHN - FFCLRP ; CIANCAGLINI, PIETRO - FFCLRP
- Unidade: FFCLRP
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Programa e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
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ABNT
RIGOS, C. F. et al. Thermal denaturation of the Na,K-ATPase solubilized and incorporated in DPPC:DPPE-liposomes. 2005, Anais.. São Paulo: SBBq, 2005. . Acesso em: 27 jan. 2026. -
APA
Rigos, C. F., Santos, H. L., Lopes, M. L., Ward, R. J., & Ciancaglini, P. (2005). Thermal denaturation of the Na,K-ATPase solubilized and incorporated in DPPC:DPPE-liposomes. In Programa e Resumos. São Paulo: SBBq. -
NLM
Rigos CF, Santos HL, Lopes ML, Ward RJ, Ciancaglini P. Thermal denaturation of the Na,K-ATPase solubilized and incorporated in DPPC:DPPE-liposomes. Programa e Resumos. 2005 ;[citado 2026 jan. 27 ] -
Vancouver
Rigos CF, Santos HL, Lopes ML, Ward RJ, Ciancaglini P. Thermal denaturation of the Na,K-ATPase solubilized and incorporated in DPPC:DPPE-liposomes. Programa e Resumos. 2005 ;[citado 2026 jan. 27 ] - Influence of enzyme conformational changes on catalytic activity of solubilized Na,K-ATPase investigated by circular dichroism spectroscopy
- Estabilidade térmica da Na, K-ATPase solubilizada e incorporada em lipossomos de DPPC:DPPE
- pH effects in Na, K-ATPase: catalytic activity, fluorescence and circular dichroism analysis
- Stability of '('alfa''beta') IND. 2' form of Na, K-ATPase: conformational states in the presence of chemical agents and thermal denaturation
- Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE
- Influence of enzyme conformational changes catalytic activity investigated by circular dichroism spectroscopy
- The study of the association of the ('alfa''beta) protomer of Na, K-ATPase solubilized with 'C IND.12''E IND. 8'
- Circular dichroism associated with surface tension and dilatational elasticity to study the association of NA,K-ATPase subunits
- The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity
- Relação estrutura/ função de proteínas
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