Peptide-lipid bilayer interaction: a comparison of the native melanotropic hormone 'ALFA'-msh to a biologically more potent analog (1995)
- Autores:
- Autores USP: NASCIMENTO, OTACIRO RANGEL - IFSC ; FREUND, MARIA TERESA LAMY - IF
- Unidades: IFSC; IF
- Assunto: BIOFÍSICA
- Idioma: Inglês
- Imprenta:
- Editora: Sociedade Brasileira de Fisica
- Local: Sao Paulo
- Data de publicação: 1995
- Fonte:
- Título do periódico: Resumos
- Nome do evento: Encontro Nacional de Fisica da Materia Condensada
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ABNT
BIAGGI, Márcia Helena et al. Peptide-lipid bilayer interaction: a comparison of the native melanotropic hormone 'ALFA'-msh to a biologically more potent analog. 1995, Anais.. Sao Paulo: Sociedade Brasileira de Fisica, 1995. . Acesso em: 28 mar. 2024. -
APA
Biaggi, M. H., Riske, K. A., Lamy, M. T. M., & Nascimento, O. R. (1995). Peptide-lipid bilayer interaction: a comparison of the native melanotropic hormone 'ALFA'-msh to a biologically more potent analog. In Resumos. Sao Paulo: Sociedade Brasileira de Fisica. -
NLM
Biaggi MH, Riske KA, Lamy MTM, Nascimento OR. Peptide-lipid bilayer interaction: a comparison of the native melanotropic hormone 'ALFA'-msh to a biologically more potent analog. Resumos. 1995 ;[citado 2024 mar. 28 ] -
Vancouver
Biaggi MH, Riske KA, Lamy MTM, Nascimento OR. Peptide-lipid bilayer interaction: a comparison of the native melanotropic hormone 'ALFA'-msh to a biologically more potent analog. Resumos. 1995 ;[citado 2024 mar. 28 ] - Probing DMPG vesicle surface with a cationic aqueous soluble spin label
- The effect of melanotropic peptides on DMPG aggregates: an ESR study with a lipid labeled at the ´16 POT.TH´ acyl chain carbon
- Characterization of DMPG vesicle surface potential by a charged water soluble spin label
- The peculiar DMPG gel-fluid transition monitored by a lipid spin-labeled at the acyl chain end
- Spin labels in the structural characterization of amphiphilic aggregates
- Probing DMPG aggregates surface with a cationic aqueous soluble spin label
- DMPG gel-fluid thermal transition monitored by a phospholipid spin labeled at the acyl chain end
- Contributions to the Gaussian line broadening of the proxyl spin probe EPR spectrum due to magnetic-field modulation and unresolved proton hyperfine structure
- Cationic amphiphiles and the solubilization of cholesterol crystallites in membrane bilayers
- Effect of the phloretin on the aggregates of negatively charged lipids: a study by electron paramagnetic resonance
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