Recognition of 'alfa'-helix transmembrane domains with an amphipatry scale generated by molecular dynamics using only the primary sequence of proteins (2007)
- Authors:
- USP affiliated authors: CIANCAGLINI, PIETRO - FFCLRP ; DEGREVE, LEO - FFCLRP
- Unidade: FFCLRP
- Assunto: GENÉTICA
- Language: Inglês
- Imprenta:
- Publisher place: Ribeirão Preto
- Date published: 2007
- Source:
- Título do periódico: Genetics and Molecular Research
- ISSN: 1676-5680
- Volume/Número/Paginação/Ano: v. 6, n. 2, p. 422-433, 2007
-
ABNT
MAZZÉ, Fernanda Marur et al. Recognition of 'alfa'-helix transmembrane domains with an amphipatry scale generated by molecular dynamics using only the primary sequence of proteins. Genetics and Molecular Research, v. 6, n. 2, p. 422-433, 2007Tradução . . Acesso em: 18 abr. 2024. -
APA
Mazzé, F. M., Fuzo, C. A., Ciancaglini, P., & Degrève, L. (2007). Recognition of 'alfa'-helix transmembrane domains with an amphipatry scale generated by molecular dynamics using only the primary sequence of proteins. Genetics and Molecular Research, 6( 2), 422-433. -
NLM
Mazzé FM, Fuzo CA, Ciancaglini P, Degrève L. Recognition of 'alfa'-helix transmembrane domains with an amphipatry scale generated by molecular dynamics using only the primary sequence of proteins. Genetics and Molecular Research. 2007 ; 6( 2): 422-433.[citado 2024 abr. 18 ] -
Vancouver
Mazzé FM, Fuzo CA, Ciancaglini P, Degrève L. Recognition of 'alfa'-helix transmembrane domains with an amphipatry scale generated by molecular dynamics using only the primary sequence of proteins. Genetics and Molecular Research. 2007 ; 6( 2): 422-433.[citado 2024 abr. 18 ] - Conformational changes of labaditin and linear analogue: interaction with lipid membrane monitored by circular Dichroism, calorimetry and molecular dynamic simulation
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