Artigo de periodico

Use of solid-state ²H NMR for studying protein-lipid interactions at emulsion interfaces (1997)

• Authors:
  • Arêas, José Alfredo Gomes
  • Gröbner, G J
  • Pellacani, L B
  • Glaubitz, C
  • Watts, A
• Autor USP: AREAS, JOSE ALFREDO GOMES - FSP
• Unidade: FSP
• DOI: 10.1002/(sici)1097-458x(199712)35:13%3Cs119::aid-omr197%3E3.0.co;2-o
• Assunto: PROTEÍNAS
• Language: Inglês
• Abstract: Interactions between myosin and beta-casein with lipids at lipid-water interfaces were studied by solid-state ²H NMR using dimyristoylphospatidylcholine with the four hydrogens at alfa- and beta-positions (DMPC-d4) and the nine protons at thegama-positions substituted by deuterium (DMPC-d9). Quadrupole splittings and spin-lattice relaxation times were used to describe the amplitude and rate of molecular motion of the choline segment, respectively, in liposomes made of pure labeleddimyristoyphosphatidylcholine or admixed with non-labeled dimyristoylphosphatidylglycerol (DMPG) in a 1:1 mole ratio. No changes were observed in these NMR parameters for the deuterons when incrasing amounts of myosin were added to liposomesexclusively made of DMPC-d9 or DMPC-d4. However, when DMPG was present, myosin was found to interact electrostatically with the liposomes, and both the quadrupolar splittings and spin-lattice relaxation times of all head -group segments wereaffected, demonstrating that DMPG was necessary in the liposomes for the interaction to occur. The results suggest that positively charged lysine residues located at the tail domain of myosin provided the necessary sites for the lipid-proteininteraction, leaving free the head domain for further structural interaction. On the other hand, beta-casein was found to interact both with the charged (with DMPG) and neutral, zwitterionic (DMPC only) liposomes, although thisinteraction wasmore pronounced in the charged lipids. In the interaction with charged liposomes, beta-casein was able to affect the lineshape of the NMR spectra from DMPC-d9 deuterons, even at low protein concentration (lipid/protein mole ratio = 30 000: 1),indicating its ability to locate at emulsion interfaces
• Imprenta:
  • Publisher place: Detroit
  • Date published: 1997
• Source:
  • Título: Magnetic Resonance in Chemistry
  • Volume/Número/Paginação/Ano: n. 35, p. S119-124, 1997

Informações sobre o DOI: 10.1002/(sici)1097-458x(199712)35:13%3Cs119::aid-omr197%3E3.0.co;2-o (Fonte: oaDOI API)
• Este periódico é de acesso aberto
• Este artigo NÃO é de acesso aberto
  

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• ABNT

  ARÊAS, José Alfredo Gomes et al. Use of solid-state ²H NMR for studying protein-lipid interactions at emulsion interfaces. Magnetic Resonance in Chemistry, n. 35, p. S119-124, 1997Tradução . . Disponível em: https://doi.org/10.1002/(sici)1097-458x(199712)35:13%3Cs119::aid-omr197%3E3.0.co;2-o. Acesso em: 14 fev. 2026.

• APA

  Arêas, J. A. G., Gröbner, G. J., Pellacani, L. B., Glaubitz, C., & Watts, A. (1997). Use of solid-state ²H NMR for studying protein-lipid interactions at emulsion interfaces. Magnetic Resonance in Chemistry, ( 35), S119-124. doi:10.1002/(sici)1097-458x(199712)35:13%3Cs119::aid-omr197%3E3.0.co;2-o

• NLM

  Arêas JAG, Gröbner GJ, Pellacani LB, Glaubitz C, Watts A. Use of solid-state ²H NMR for studying protein-lipid interactions at emulsion interfaces [Internet]. Magnetic Resonance in Chemistry. 1997 ;( 35): S119-124.[citado 2026 fev. 14 ] Available from: https://doi.org/10.1002/(sici)1097-458x(199712)35:13%3Cs119::aid-omr197%3E3.0.co;2-o

• Vancouver

  Arêas JAG, Gröbner GJ, Pellacani LB, Glaubitz C, Watts A. Use of solid-state ²H NMR for studying protein-lipid interactions at emulsion interfaces [Internet]. Magnetic Resonance in Chemistry. 1997 ;( 35): S119-124.[citado 2026 fev. 14 ] Available from: https://doi.org/10.1002/(sici)1097-458x(199712)35:13%3Cs119::aid-omr197%3E3.0.co;2-o

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