Filtros : "Secondary structure" Limpar

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  • Source: Chemistry and Physics of Lipids. Unidade: IFSC

    Subjects: FILMES FINOS, NEOPLASIAS, NANOTECNOLOGIA, MEMBRANA PLASMÁTICA

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    • ABNT

      SANDRINO, Bianca et al. The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract. Chemistry and Physics of Lipids, v. 230, p. 104930-1-104930-7, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.chemphyslip.2020.104930. Acesso em: 07 jan. 2026.
    • APA

      Sandrino, B., Jochelavicius, K., Volpati, D., Barbosa, S. C., Nobre, T. M., & Oliveira Junior, O. N. de. (2020). The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract. Chemistry and Physics of Lipids, 230, 104930-1-104930-7. doi:10.1016/j.chemphyslip.2020.104930
    • NLM

      Sandrino B, Jochelavicius K, Volpati D, Barbosa SC, Nobre TM, Oliveira Junior ON de. The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract [Internet]. Chemistry and Physics of Lipids. 2020 ; 230 104930-1-104930-7.[citado 2026 jan. 07 ] Available from: https://doi.org/10.1016/j.chemphyslip.2020.104930
    • Vancouver

      Sandrino B, Jochelavicius K, Volpati D, Barbosa SC, Nobre TM, Oliveira Junior ON de. The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract [Internet]. Chemistry and Physics of Lipids. 2020 ; 230 104930-1-104930-7.[citado 2026 jan. 07 ] Available from: https://doi.org/10.1016/j.chemphyslip.2020.104930
  • Source: Protein Science. Unidade: IFSC

    Subjects: RADIAÇÃO SINCROTRON, PROTEÍNAS

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    • ABNT

      YONEDA, Juliana Sakamoto et al. Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation. Protein Science, v. 26, n. 4, p. 718-726, 2017Tradução . . Disponível em: https://doi.org/10.1002/pro.3118. Acesso em: 07 jan. 2026.
    • APA

      Yoneda, J. S., Miles, A. J., Araújo, A. P. U. de, & Wallace, B. A. (2017). Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation. Protein Science, 26( 4), 718-726. doi:10.1002/pro.3118
    • NLM

      Yoneda JS, Miles AJ, Araújo APU de, Wallace BA. Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation [Internet]. Protein Science. 2017 ; 26( 4): 718-726.[citado 2026 jan. 07 ] Available from: https://doi.org/10.1002/pro.3118
    • Vancouver

      Yoneda JS, Miles AJ, Araújo APU de, Wallace BA. Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation [Internet]. Protein Science. 2017 ; 26( 4): 718-726.[citado 2026 jan. 07 ] Available from: https://doi.org/10.1002/pro.3118
  • Source: European Biophysics Journal. Unidades: IFSC, IF

    Subjects: PROTEÍNAS, CRISTALOGRAFIA, MEMBRANAS CELULARES

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    • ABNT

      KUMAGAI, Patricia S. e DE MARCO, Ricardo e LOPES, José luiz de Souza. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. European Biophysics Journal, v. 46, n. 7, p. 599-606, 2017Tradução . . Disponível em: https://doi.org/10.1007/s00249-017-1202-1. Acesso em: 07 jan. 2026.
    • APA

      Kumagai, P. S., De Marco, R., & Lopes, J. luiz de S. (2017). Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. European Biophysics Journal, 46( 7), 599-606. doi:10.1007/s00249-017-1202-1
    • NLM

      Kumagai PS, De Marco R, Lopes J luiz de S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins [Internet]. European Biophysics Journal. 2017 ; 46( 7): 599-606.[citado 2026 jan. 07 ] Available from: https://doi.org/10.1007/s00249-017-1202-1
    • Vancouver

      Kumagai PS, De Marco R, Lopes J luiz de S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins [Internet]. European Biophysics Journal. 2017 ; 46( 7): 599-606.[citado 2026 jan. 07 ] Available from: https://doi.org/10.1007/s00249-017-1202-1

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