The C-terminal fragment of acanthoscurrin is a difficult sequence (2005)
- Authors:
- USP affiliated authors: TEMPERINI, MARCIA LAUDELINA ARRUDA - IQ ; DAFFRE, SIRLEI - ICB ; MIRANDA, MARIA TERESA MACHINI DE - IQ
- Unidades: IQ; ICB
- Assunto: PARASITOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Biopolymers
- ISSN: 0006-3525
- Volume/Número/Paginação/Ano: v. 80, p. 520, res. P-018, 2005
- Conference titles: American Peptide Symposium
-
ABNT
REMUZGO, C. et al. The C-terminal fragment of acanthoscurrin is a difficult sequence. Biopolymers. New York: Instituto de Química, Universidade de São Paulo. . Acesso em: 04 out. 2024. , 2005 -
APA
Remuzgo, C., Andrade, G. F. S., Temperini, M. L. A., Daffre, S., & Miranda, M. T. M. de. (2005). The C-terminal fragment of acanthoscurrin is a difficult sequence. Biopolymers. New York: Instituto de Química, Universidade de São Paulo. -
NLM
Remuzgo C, Andrade GFS, Temperini MLA, Daffre S, Miranda MTM de. The C-terminal fragment of acanthoscurrin is a difficult sequence. Biopolymers. 2005 ; 80 520.[citado 2024 out. 04 ] -
Vancouver
Remuzgo C, Andrade GFS, Temperini MLA, Daffre S, Miranda MTM de. The C-terminal fragment of acanthoscurrin is a difficult sequence. Biopolymers. 2005 ; 80 520.[citado 2024 out. 04 ] - Antimicrobial activity of lactam bridge gomesin analogues
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- Solution structure of an antimicrobial peptide derive from bovine hemoglobin by CD and NMR spectroscopy
- Importance of the intramolecular disulfide bridges in the biological activity of gomesin
- Linear analogues of gomesin: design and structure activity relationship
- CD, NMR and biological studies of linear gomesin analogue
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