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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
26/01/2012 |
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Data da última atualização: |
24/01/2020 |
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Tipo da produção científica: |
Artigo em Anais de Congresso |
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Autoria: |
DUARTE, F.; SEPULVEDA, R.; ARAYA, R.; FLORES, S.; PEREZ-ACLE, T.; GONZALES, W.; GONZALES, D.; NESHICH, G.; NESHICH, I.; MAZONI, I.; HOLMES, D. S. |
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Afiliação: |
FRANCISCO DUARTE, Universidad Andres Bello; RENE SEPULVEDA, Universidad Andres Bello; RAUL ARAYA, Universidad de Chile; SEBASTIAN FLORES, Universidad de Chile; TOMAS PEREZ-ACLE, Universidad de Chile; WENDY GONZALES, Universidad de Talca; DANILO GONZALES, Universidad de Talca; GORAN NESHICH, CNPTIA; IZABELLA NESHICH, Embrapa, Unicamp; IVAN MAZONI, CNPTIA; DAVID S. HOLMES, Universidad Andres Bello. |
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Título: |
Mechanisms of protein stabilization at very low pH. |
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Ano de publicação: |
2011 |
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Fonte/Imprenta: |
In: INTERNATIONAL BIOHYDROMETALLURGY SYMPOSIUM, 19.; 2011, Changsha, China. Biohydrometallurgy: biotech key to unlock mineral resources value: proceedings. Changsha: Central South University Press, 2011. |
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Volume: |
v. 1. |
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Descrição Física: |
IBS 2011. |
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Idioma: |
Inglês |
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Conteúdo: |
Physicochemical properties of periplasmic loops exposed to low pH were determined for two membrane proteins from the bioleaching-proteobacterium Acidithiobacillus ferrooxidans. The selected proteins were an aquaporin and a potassium (K+) channel and the properties evaluated were surface area hydrophobicity and amino acid composition. Properties were mapped onto three dimensional protein models and subjected to Accessible Surface Area (ASA) analysis and Molecular Dynamics (MD) simulations. Results were compared to equivalent loops from homologous proteins derived from microorganisms that live in neutral pH environments. It was found that periplasmic loops of both the aquaporin and the K+ channel protein of At ferrooxidans have less surface area and exhibit greater hydrophobicity compared to their neutrophilic homologs. A reduction of the percentage of amino acids that are negatively charged (aspartic and glutamic acid) and an increase in the percentage of positively charged amino acids (histidine, arginine and lysine) was also observed in the periplasmic loops of the aquaporin and potassium (K+) channel of At ferrooxidans. Finally, an increase in the proline content of the loops of At ferrooxidans was detected. Hypotheses for how these features could help stabilize the structure and function of proteins in extremely acidic condition are presented. It is noted that these proposed mechanisms are similar to those shown to be operational for the stabilization of thermophilic proteins. The data and hypotheses presented could help provide a theoretical foundation for designing proteins with improved molecular functions for bioleaching and acid mine drainage remediation. It is also valuable information for understanding the molecular underpinnings and evolution of protein function at low pH. MenosPhysicochemical properties of periplasmic loops exposed to low pH were determined for two membrane proteins from the bioleaching-proteobacterium Acidithiobacillus ferrooxidans. The selected proteins were an aquaporin and a potassium (K+) channel and the properties evaluated were surface area hydrophobicity and amino acid composition. Properties were mapped onto three dimensional protein models and subjected to Accessible Surface Area (ASA) analysis and Molecular Dynamics (MD) simulations. Results were compared to equivalent loops from homologous proteins derived from microorganisms that live in neutral pH environments. It was found that periplasmic loops of both the aquaporin and the K+ channel protein of At ferrooxidans have less surface area and exhibit greater hydrophobicity compared to their neutrophilic homologs. A reduction of the percentage of amino acids that are negatively charged (aspartic and glutamic acid) and an increase in the percentage of positively charged amino acids (histidine, arginine and lysine) was also observed in the periplasmic loops of the aquaporin and potassium (K+) channel of At ferrooxidans. Finally, an increase in the proline content of the loops of At ferrooxidans was detected. Hypotheses for how these features could help stabilize the structure and function of proteins in extremely acidic condition are presented. It is noted that these proposed mechanisms are similar to those shown to be operational for the stabilization of thermophilic prot... Mostrar Tudo |
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Palavras-Chave: |
Aquaporinas; Canal de potássio; Estabilização de proteínas a pH baixo. |
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Thesaurus Nal: |
Acidithiobacillus ferrooxidans; Aquaporins; Potassium channels; Proteins. |
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Categoria do assunto: |
S Ciências Biológicas |
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Marc: |
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Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
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| Registros recuperados : 6 | |
| 4. |  | DUARTE, G. da S.; PERES, M. M.; CORRÊA, B. O.; PIRES, G. da S.; STUMPF, M. M.; MITTELMANN, A. Avaliação de caracteres relacionados ao potencial produtivo em acessos de Capim-elefante. In: REUNIÓN DEL GRUPO TÉCNICO EN FORRAJERAS DEL CONO SUR GRUPO CAMPOS, 22., 2008, Minas. Resumos...Minas: INIA, 2008. 1 CD-ROM.| Tipo: Artigo em Anais de Congresso / Nota Técnica |
| Biblioteca(s): Embrapa Clima Temperado. |
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| 5. | | PERES, M. M.; DUARTE, G. da S.; MITTELMANN, A.; PEREIRA, A. V.; LEDO, F. J. da S. Produtividade de genótipos de capim-elefante. In: CONGRESSO DE INICIAÇÃO CIENTÍFICA, 2.; ENCONTRO DE PÓS GRADUAÇÃO DA EMBRAPA CLIMA TEMPERADO, 2., 2008, Pelotas. anais... Pelotas: Embrapa Clima Temperado, 2008. p. 59 Volume 1.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Clima Temperado. |
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| 6. | | DUARTE, G. da S.; FERREIRA, O. G. L.; SILVA, J. L. S. da; MACARI, S.; COSTA, O. A. D.; FARIAS, P. P.; KRÖNING, A. B. Desempenho de um sistema integrado de produção agropecuária sobre pastagem de inverno. Revista Científica Rural, v.1, n. 2, 2017.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 4 |
| Biblioteca(s): Embrapa Clima Temperado. |
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| Registros recuperados : 6 | |
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