Force-induced chemical reactions on the metal centre in a single metalloprotein molecule (2015)
- Authors:
- Autor USP: ARANTES, GUILHERME MENEGON - IQ
- Unidade: IQ
- DOI: 10.1038/ncomms8569
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Nature Communications
- ISSN: 2041-1723
- Volume/Número/Paginação/Ano: v. 6, p. 7569-7577, 2015
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: gold
- Licença: cc-by
-
ABNT
ZHENG, Peng et al. Force-induced chemical reactions on the metal centre in a single metalloprotein molecule. Nature Communications, v. 6, p. 7569-7577, 2015Tradução . . Disponível em: https://doi.org/10.1038/ncomms8569. Acesso em: 12 jun. 2025. -
APA
Zheng, P., Arantes, G. M., Field, M. J., & Li, H. (2015). Force-induced chemical reactions on the metal centre in a single metalloprotein molecule. Nature Communications, 6, 7569-7577. doi:10.1038/ncomms8569 -
NLM
Zheng P, Arantes GM, Field MJ, Li H. Force-induced chemical reactions on the metal centre in a single metalloprotein molecule [Internet]. Nature Communications. 2015 ; 6 7569-7577.[citado 2025 jun. 12 ] Available from: https://doi.org/10.1038/ncomms8569 -
Vancouver
Zheng P, Arantes GM, Field MJ, Li H. Force-induced chemical reactions on the metal centre in a single metalloprotein molecule [Internet]. Nature Communications. 2015 ; 6 7569-7577.[citado 2025 jun. 12 ] Available from: https://doi.org/10.1038/ncomms8569 - Computational molecular bioenergetics: simulations of iron-sulfur proteins and mobile natural quinones
- Computational method to cluster complexes of small ligands and flexible proteins
- Mechanism of bond dissociation in metalloproteins under stress
- Effects of lipid composition on membrane distribution and permeability of natural quinones
- Parametrization of an ubiquinone force field and simulation of membrane partition, diffusion and redox potentials
- Ligand receptor affinities computed by an adapted linear interaction model for continuum electrostatics and by protein conformational averaging
- Computational molecular bioenergetics: simulations of iron-sulfur proteins and respiratory complexes
- Hydride transfer from flavin cofactors as a multiconfigurational electronic process
- Approximate multiconfigurational treatment of spin-coupled metal complexes
- Resenha sem título próprio
Informações sobre o DOI: 10.1038/ncomms8569 (Fonte: oaDOI API)
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