Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane (2013)
- Authors:
- Autor USP: SCHREIER, SHIRLEY - IQ
- Unidade: IQ
- DOI: 10.1002/bip.22211
- Subjects: FLUORESCÊNCIA; PEPTÍDEOS
- Language: Inglês
- Imprenta:
- Source:
- Título: Biopolymers
- ISSN: 0006-3525
- Volume/Número/Paginação/Ano: v. 100, n. 4, p. 337-346, 2013
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
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ABNT
ROS, Uris et al. Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane. Biopolymers, v. 100, n. 4, p. 337-346, 2013Tradução . . Disponível em: https://doi.org/10.1002/bip.22211. Acesso em: 29 jan. 2026. -
APA
Ros, U., Souto, A. L. C. F., Oliveira, F. J. de, Crusca Junior, E., Pazos, F., Cilli, E. M., et al. (2013). Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane. Biopolymers, 100( 4), 337-346. doi:10.1002/bip.22211 -
NLM
Ros U, Souto ALCF, Oliveira FJ de, Crusca Junior E, Pazos F, Cilli EM, Lanio ME, Schreier S, Alvarez C. Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane [Internet]. Biopolymers. 2013 ; 100( 4): 337-346.[citado 2026 jan. 29 ] Available from: https://doi.org/10.1002/bip.22211 -
Vancouver
Ros U, Souto ALCF, Oliveira FJ de, Crusca Junior E, Pazos F, Cilli EM, Lanio ME, Schreier S, Alvarez C. Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane [Internet]. Biopolymers. 2013 ; 100( 4): 337-346.[citado 2026 jan. 29 ] Available from: https://doi.org/10.1002/bip.22211 - Spin label study of local anesthetic-lipid membrane interactions. Phase separation of the uncharged form and bilayer micellization by the charged form of tetracaine cellization by the charged form of tetracaine
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Informações sobre o DOI: 10.1002/bip.22211 (Fonte: oaDOI API)
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