LMProt: and efficient algorithm for Monte Carlo sampling of protein conformational space (2004)
- Authors:
- USP affiliated authors: DEGREVE, LEO - FFCLRP ; CALIRI, ANTONIO - FCFRP
- Unidades: FFCLRP; FCFRP
- Assunto: FÍSICO-QUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Biophysical Journal
- ISSN: 0006-3495
- Volume/Número/Paginação/Ano: v. 87, n. 3, p. 1-11, 2004
-
ABNT
SILVA, Roosevelt Alves da e DEGRÈVE, Léo e CALIRI, Antônio. LMProt: and efficient algorithm for Monte Carlo sampling of protein conformational space. Biophysical Journal, v. 87, n. 3, p. 1-11, 2004Tradução . . Acesso em: 12 jun. 2025. -
APA
Silva, R. A. da, Degrève, L., & Caliri, A. (2004). LMProt: and efficient algorithm for Monte Carlo sampling of protein conformational space. Biophysical Journal, 87( 3), 1-11. -
NLM
Silva RA da, Degrève L, Caliri A. LMProt: and efficient algorithm for Monte Carlo sampling of protein conformational space. Biophysical Journal. 2004 ; 87( 3): 1-11.[citado 2025 jun. 12 ] -
Vancouver
Silva RA da, Degrève L, Caliri A. LMProt: and efficient algorithm for Monte Carlo sampling of protein conformational space. Biophysical Journal. 2004 ; 87( 3): 1-11.[citado 2025 jun. 12 ] - Molecular simulation of the E protein from dengue virus type 2
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- Extensive structural change of the envelope protein of dengue virus induced by a tuned ionic strength: conformational and energetic analyses
- The role of disulfide bridges in the 3-D structures of the antimicrobial peptides gomesin and protegrin-1: a molecular dynamics study
- Cobra: um algoritmo Monte Carlo ideal para enovelar proteínas
- Um super computador no combate ao dengue. [Depoimento à Rosemeire Talamone]
- The stability of extended secondary protein structures: the Dengue virus E protein case
- Geometric constraints in polymer chains: analysis on the pearl-necklace model by monte carlo simulation
- The ionic strength is also responsible for structural changes in proteins
- Extended secondary structures in proteins
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