| |
|
|
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Meio Ambiente. |
|
Data corrente: |
23/02/2015 |
|
Data da última atualização: |
30/10/2019 |
|
Tipo da produção científica: |
Artigo em Anais de Congresso |
|
Autoria: |
PACKER, A. P.; DEGASPARI, I. A. M.; MORASI, I. M.; VILELA, V. A. A.; MAXIMILIANO, V. C. B.; SANTOS, J. de O.; RAMOS, N. P.; CABRAL, O. M. R.; ROSETTO, R. |
|
Afiliação: |
ANA PAULA CONTADOR PACKER, CNPMA; IRACEMA A M DEGASPARI; IGOR MARTINS MORASI, PUCCAMP; VIVIANE APARECIDA ALVES VILELA, PUCCAMP; VIVIANE CRISTINA B MAXIMILIANO, CNPMA; JULIANA DE OLIVEIRA SANTOS, CNPMA; NILZA PATRICIA RAMOS, CNPMA; OSVALDO MACHADO RODRIGUES CABRAL, CNPMA; RAFFAELLA ROSETTO, APTA Piracicaba. |
|
Título: |
Site-specific N2O emission from soil related to fertilization and sugarcane trash addition. |
|
Ano de publicação: |
2014 |
|
Fonte/Imprenta: |
In: WORLD FERTILIZER CONGRESS OF CIEC, 16., 2014, Rio de Janeiro. Technological innovation for a sustainable tropical agriculture: proceedings. Rio de Janeiro: International Scientific Centre of Fertilizers, 2014. p. 305-307. |
|
Idioma: |
Inglês |
|
Palavras-Chave: |
Fertilização; Fertilizar application. |
|
Thesagro: |
Cana de açucar; Resíduo orgânico. |
|
Thesaurus Nal: |
Crop residues; Nitrous oxide; Straw; Sugarcane. |
|
Categoria do assunto: |
P Recursos Naturais, Ciências Ambientais e da Terra |
|
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/118410/1/2014AA74.pdf
|
|
Marc: |
LEADER 01036nam a2200289 a 4500
001 2009300
005 2019-10-30
008 2014 bl uuuu u00u1 u #d
100 1 $aPACKER, A. P.
245 $aSite-specific N2O emission from soil related to fertilization and sugarcane trash addition.$h[electronic resource]
260 $aIn: WORLD FERTILIZER CONGRESS OF CIEC, 16., 2014, Rio de Janeiro. Technological innovation for a sustainable tropical agriculture: proceedings. Rio de Janeiro: International Scientific Centre of Fertilizers, 2014. p. 305-307.$c2014
650 $aCrop residues
650 $aNitrous oxide
650 $aStraw
650 $aSugarcane
650 $aCana de açucar
650 $aResíduo orgânico
653 $aFertilização
653 $aFertilizar application
700 1 $aDEGASPARI, I. A. M.
700 1 $aMORASI, I. M.
700 1 $aVILELA, V. A. A.
700 1 $aMAXIMILIANO, V. C. B.
700 1 $aSANTOS, J. de O.
700 1 $aRAMOS, N. P.
700 1 $aCABRAL, O. M. R.
700 1 $aROSETTO, R.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Meio Ambiente (CNPMA) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
Registro Completo
|
Biblioteca(s): |
Embrapa Agricultura Digital. |
|
Data corrente: |
07/12/2007 |
|
Data da última atualização: |
11/05/2017 |
|
Tipo da produção científica: |
Artigo em Periódico Indexado |
|
Circulação/Nível: |
Internacional - A |
|
Autoria: |
ROCCHIA, W.; NESHICH, G. |
|
Afiliação: |
Scuola Normale Superiore, Italy; GORAN NESHICH, CNPTIA. |
|
Título: |
Electrostatic potential calculation for biomolecules - creating a database of pré-calculated values reported on a per residue basis for all PDB protein structures. |
|
Ano de publicação: |
2007 |
|
Fonte/Imprenta: |
Genetics and Molecular Research, v. 6, n. 4, p. 923-936, 2007. |
|
Idioma: |
Inglês |
|
Conteúdo: |
Abstract. STING and JavaProtein Dossier provide a collection of physical-chemical parameters, describing protein structure, stability, function, and interaction, considered one of the most comprehensive among the available protein databases of similar type. Particular attention in STING is paid to the electrostatic potential. It makes use of DelPhi, a well-known tool that calculates this physical-chemical quantity for biomolecules by solving the Poisson Boltzmann equation. In this paper, we describe a modification to the DelPhi program aimed at integrating it within the STING environment. We also outline how the "amino acid electrostatic potential" and the "surface amino acid electrostatic potential" are calculated (over all Protein Data Bank (PDB) content) and how the corresponding values are made searchable in STING_DB. In addition, we show that the STING and JavaProtein Dossier are also capable of providing these particular parameter values for the analysis of protein structures modeled in computers or being experimentally solved, but not yet deposited in the PDB. Furthermore, we compare the calculated electrostatic potential values obtained by using the earlier version of DelPhi and those by STING, for the biologically relevant case of lysozyme-antibody interaction. Finally, we describe the STING capacity to make queries (at both residue and atomic levels) across the whole PDB, by looking at a specific case where the electrostatic potential parameter plays a crucial role in terms of a particular protein function, such as ligand binding. MenosAbstract. STING and JavaProtein Dossier provide a collection of physical-chemical parameters, describing protein structure, stability, function, and interaction, considered one of the most comprehensive among the available protein databases of similar type. Particular attention in STING is paid to the electrostatic potential. It makes use of DelPhi, a well-known tool that calculates this physical-chemical quantity for biomolecules by solving the Poisson Boltzmann equation. In this paper, we describe a modification to the DelPhi program aimed at integrating it within the STING environment. We also outline how the "amino acid electrostatic potential" and the "surface amino acid electrostatic potential" are calculated (over all Protein Data Bank (PDB) content) and how the corresponding values are made searchable in STING_DB. In addition, we show that the STING and JavaProtein Dossier are also capable of providing these particular parameter values for the analysis of protein structures modeled in computers or being experimentally solved, but not yet deposited in the PDB. Furthermore, we compare the calculated electrostatic potential values obtained by using the earlier version of DelPhi and those by STING, for the biologically relevant case of lysozyme-antibody interaction. Finally, we describe the STING capacity to make queries (at both residue and atomic levels) across the whole PDB, by looking at a specific case where the electrostatic potential parameter plays a crucial role... Mostrar Tudo |
|
Palavras-Chave: |
Banco de dados; Bioinformática; Biomoléculas; Electrostatic potential of biomolecules; Protein structure analysis; Sting. |
|
Thesagro: |
Proteína. |
|
Thesaurus NAL: |
Bioinformatics; Protein structure. |
|
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
|
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/159699/1/AP-Electrostatic-Sting-GMR-2007.pdf
|
|
Marc: |
LEADER 02370naa a2200241 a 4500
001 1000899
005 2017-05-11
008 2007 bl uuuu u00u1 u #d
100 1 $aROCCHIA, W.
245 $aElectrostatic potential calculation for biomolecules - creating a database of pré-calculated values reported on a per residue basis for all PDB protein structures.$h[electronic resource]
260 $c2007
520 $aAbstract. STING and JavaProtein Dossier provide a collection of physical-chemical parameters, describing protein structure, stability, function, and interaction, considered one of the most comprehensive among the available protein databases of similar type. Particular attention in STING is paid to the electrostatic potential. It makes use of DelPhi, a well-known tool that calculates this physical-chemical quantity for biomolecules by solving the Poisson Boltzmann equation. In this paper, we describe a modification to the DelPhi program aimed at integrating it within the STING environment. We also outline how the "amino acid electrostatic potential" and the "surface amino acid electrostatic potential" are calculated (over all Protein Data Bank (PDB) content) and how the corresponding values are made searchable in STING_DB. In addition, we show that the STING and JavaProtein Dossier are also capable of providing these particular parameter values for the analysis of protein structures modeled in computers or being experimentally solved, but not yet deposited in the PDB. Furthermore, we compare the calculated electrostatic potential values obtained by using the earlier version of DelPhi and those by STING, for the biologically relevant case of lysozyme-antibody interaction. Finally, we describe the STING capacity to make queries (at both residue and atomic levels) across the whole PDB, by looking at a specific case where the electrostatic potential parameter plays a crucial role in terms of a particular protein function, such as ligand binding.
650 $aBioinformatics
650 $aProtein structure
650 $aProteína
653 $aBanco de dados
653 $aBioinformática
653 $aBiomoléculas
653 $aElectrostatic potential of biomolecules
653 $aProtein structure analysis
653 $aSting
700 1 $aNESHICH, G.
773 $tGenetics and Molecular Research$gv. 6, n. 4, p. 923-936, 2007.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
Fechar
|
| Nenhum registro encontrado para a expressão de busca informada. |
|
|
