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Artigo de periodico
Understanding the Fe-CO bond through the electronic structure of Fem+(CO)6-nLn, m = 2, 3, n = 0–3, L = Cl−, Br−, H2O or NH3 (2021)
Pelegrini, Marina; Galembeck, Sérgio Emanuel
Fonte: Journal of Molecular Modeling. Unidade: FFCLRP
Assuntos: MONÓXIDO DE CARBONO, LIGANTES, QUÍMICA QUÂNTICA, ORBITAL MOLECULAR
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ABNT
PELEGRINI, Marina e GALEMBECK, Sérgio Emanuel. Understanding the Fe-CO bond through the electronic structure of Fem+(CO)6-nLn, m = 2, 3, n = 0–3, L = Cl−, Br−, H2O or NH3. Journal of Molecular Modeling, v. 27, n. 5, 2021Tradução . . Disponível em: https://doi.org/10.1007/s00894-021-04744-x. Acesso em: 09 nov. 2025.
APA
Pelegrini, M., & Galembeck, S. E. (2021). Understanding the Fe-CO bond through the electronic structure of Fem+(CO)6-nLn, m = 2, 3, n = 0–3, L = Cl−, Br−, H2O or NH3. Journal of Molecular Modeling, 27( 5). doi:10.1007/s00894-021-04744-x
NLM
Pelegrini M, Galembeck SE. Understanding the Fe-CO bond through the electronic structure of Fem+(CO)6-nLn, m = 2, 3, n = 0–3, L = Cl−, Br−, H2O or NH3 [Internet]. Journal of Molecular Modeling. 2021 ; 27( 5):[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-021-04744-x
Vancouver
Pelegrini M, Galembeck SE. Understanding the Fe-CO bond through the electronic structure of Fem+(CO)6-nLn, m = 2, 3, n = 0–3, L = Cl−, Br−, H2O or NH3 [Internet]. Journal of Molecular Modeling. 2021 ; 27( 5):[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-021-04744-x
Artigo de periodico
Shedding light on the electronic structure of [Ru(η6-C16H16)(NH3)3]2+ complex: a computational insight (2019)
Orenha, Renato Pereira; Caramori, Giovanni Finoto; Misturini, Alechania; Galembeck, Sérgio Emanuel
Fonte: Journal of Molecular Modeling. Unidade: FFCLRP
Assuntos: LIGAÇÕES QUÍMICAS, ESTRUTURA ELETRÔNICA, COMPUTAÇÃO APLICADA
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ABNT
ORENHA, Renato Pereira et al. Shedding light on the electronic structure of [Ru(η6-C16H16)(NH3)3]2+ complex: a computational insight. Journal of Molecular Modeling, v. 25, n. 1, 2019Tradução . . Disponível em: https://doi.org/10.1007/s00894-018-3882-6. Acesso em: 09 nov. 2025.
APA
Orenha, R. P., Caramori, G. F., Misturini, A., & Galembeck, S. E. (2019). Shedding light on the electronic structure of [Ru(η6-C16H16)(NH3)3]2+ complex: a computational insight. Journal of Molecular Modeling, 25( 1). doi:10.1007/s00894-018-3882-6
NLM
Orenha RP, Caramori GF, Misturini A, Galembeck SE. Shedding light on the electronic structure of [Ru(η6-C16H16)(NH3)3]2+ complex: a computational insight [Internet]. Journal of Molecular Modeling. 2019 ; 25( 1):[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-018-3882-6
Vancouver
Orenha RP, Caramori GF, Misturini A, Galembeck SE. Shedding light on the electronic structure of [Ru(η6-C16H16)(NH3)3]2+ complex: a computational insight [Internet]. Journal of Molecular Modeling. 2019 ; 25( 1):[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-018-3882-6
Artigo de periodico
Synergistic long-range effects of mutations underlie aggregation propensities of amylin analogues (2019)
Alves, Nelson Augusto ; Dias, Luis Gustavo ; Frigori, Rafael Bertolini
Fonte: Journal of Molecular Modeling. Unidade: FFCLRP
Assuntos: TERMODINÂMICA (FÍSICO-QUÍMICA), SOLVATAÇÃO, ENERGIA
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ABNT
ALVES, Nelson Augusto e DIAS, Luis Gustavo e FRIGORI, Rafael Bertolini. Synergistic long-range effects of mutations underlie aggregation propensities of amylin analogues. Journal of Molecular Modeling, v. 25, n. 9, 2019Tradução . . Disponível em: https://doi.org/10.1007/s00894-019-4137-x. Acesso em: 09 nov. 2025.
APA
Alves, N. A., Dias, L. G., & Frigori, R. B. (2019). Synergistic long-range effects of mutations underlie aggregation propensities of amylin analogues. Journal of Molecular Modeling, 25( 9). doi:10.1007/s00894-019-4137-x
NLM
Alves NA, Dias LG, Frigori RB. Synergistic long-range effects of mutations underlie aggregation propensities of amylin analogues [Internet]. Journal of Molecular Modeling. 2019 ; 25( 9):[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-019-4137-x
Vancouver
Alves NA, Dias LG, Frigori RB. Synergistic long-range effects of mutations underlie aggregation propensities of amylin analogues [Internet]. Journal of Molecular Modeling. 2019 ; 25( 9):[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-019-4137-x
Artigo de periodico
Effects of the protonation state in the interaction of an HIV-1 reverse transcriptase (RT) amino acid, Lys101, and a non nucleoside RT inhibitor, GW420867X (2014)
Galembeck, Sergio Emanuel; Bickelhaupt, F. Matthias; Guerra, Célia Fonseca; Galembeck, Eduardo
Fonte: Journal of Molecular Modeling. Unidade: FFCLRP
Assuntos: SÍNDROME DE IMUNODEFICIÊNCIA ADQUIRIDA, HIV
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
GALEMBECK, Sergio Emanuel et al. Effects of the protonation state in the interaction of an HIV-1 reverse transcriptase (RT) amino acid, Lys101, and a non nucleoside RT inhibitor, GW420867X. Journal of Molecular Modeling, v. 20, n. 7, p. 2332-1-2332-11, 2014Tradução . . Disponível em: https://doi.org/10.1007/s00894-014-2332-3. Acesso em: 09 nov. 2025.
APA
Galembeck, S. E., Bickelhaupt, F. M., Guerra, C. F., & Galembeck, E. (2014). Effects of the protonation state in the interaction of an HIV-1 reverse transcriptase (RT) amino acid, Lys101, and a non nucleoside RT inhibitor, GW420867X. Journal of Molecular Modeling, 20( 7), 2332-1-2332-11. doi:10.1007/s00894-014-2332-3
NLM
Galembeck SE, Bickelhaupt FM, Guerra CF, Galembeck E. Effects of the protonation state in the interaction of an HIV-1 reverse transcriptase (RT) amino acid, Lys101, and a non nucleoside RT inhibitor, GW420867X [Internet]. Journal of Molecular Modeling. 2014 ; 20( 7): 2332-1-2332-11.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-014-2332-3
Vancouver
Galembeck SE, Bickelhaupt FM, Guerra CF, Galembeck E. Effects of the protonation state in the interaction of an HIV-1 reverse transcriptase (RT) amino acid, Lys101, and a non nucleoside RT inhibitor, GW420867X [Internet]. Journal of Molecular Modeling. 2014 ; 20( 7): 2332-1-2332-11.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-014-2332-3
Artigo de periodico
Effect of the thermostat in the molecular dynamics simulation on the folding of the model protein chignolin (2012)
Fuzo, Carlos A.; Degrève, Léo
Fonte: Journal of Molecular Modeling. Unidade: FFCLRP
Assuntos: PROTEÍNAS (MODELOS;INTERAÇÃO), MOLÉCULA (ATIVIDADE), FÍSICO-QUÍMICA
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ABNT
FUZO, Carlos A. e DEGRÈVE, Léo. Effect of the thermostat in the molecular dynamics simulation on the folding of the model protein chignolin. Journal of Molecular Modeling, v. 18, n. 6, p. 2785-2794, 2012Tradução . . Disponível em: https://doi.org/10.1007/s00894-011-1282-2. Acesso em: 09 nov. 2025.
APA
Fuzo, C. A., & Degrève, L. (2012). Effect of the thermostat in the molecular dynamics simulation on the folding of the model protein chignolin. Journal of Molecular Modeling, 18( 6), 2785-2794. doi:10.1007/s00894-011-1282-2
NLM
Fuzo CA, Degrève L. Effect of the thermostat in the molecular dynamics simulation on the folding of the model protein chignolin [Internet]. Journal of Molecular Modeling. 2012 ; 18( 6): 2785-2794.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-011-1282-2
Vancouver
Fuzo CA, Degrève L. Effect of the thermostat in the molecular dynamics simulation on the folding of the model protein chignolin [Internet]. Journal of Molecular Modeling. 2012 ; 18( 6): 2785-2794.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-011-1282-2
Artigo de periodico
Conformation analysis of a surface loop that controls active site access in the GH11 xylananse A from Bacillus subtilis (2012)
Vieira, Davi Serradella; Ward, Richard John
Fonte: Journal of Molecular Modeling. Unidade: FFCLRP
Assuntos: BACTÉRIAS, PROTEÍNAS, ENZIMOLOGIA, FÍSICO-QUÍMICA ORGÂNICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
VIEIRA, Davi Serradella e WARD, Richard John. Conformation analysis of a surface loop that controls active site access in the GH11 xylananse A from Bacillus subtilis. Journal of Molecular Modeling, v. 18, n. 4, p. 1473-1479, 2012Tradução . . Disponível em: https://doi.org/10.1007/s00894-011-1172-7. Acesso em: 09 nov. 2025.
APA
Vieira, D. S., & Ward, R. J. (2012). Conformation analysis of a surface loop that controls active site access in the GH11 xylananse A from Bacillus subtilis. Journal of Molecular Modeling, 18( 4), 1473-1479. doi:10.1007/s00894-011-1172-7
NLM
Vieira DS, Ward RJ. Conformation analysis of a surface loop that controls active site access in the GH11 xylananse A from Bacillus subtilis [Internet]. Journal of Molecular Modeling. 2012 ; 18( 4): 1473-1479.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-011-1172-7
Vancouver
Vieira DS, Ward RJ. Conformation analysis of a surface loop that controls active site access in the GH11 xylananse A from Bacillus subtilis [Internet]. Journal of Molecular Modeling. 2012 ; 18( 4): 1473-1479.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1007/s00894-011-1172-7

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