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Registro Completo |
Biblioteca(s): |
Embrapa Agricultura Digital. |
Data corrente: |
26/11/2009 |
Data da última atualização: |
15/01/2020 |
Tipo da produção científica: |
Resumo em Anais de Congresso |
Autoria: |
MAZONI, I.; BORRO, L. C.; MANCINI, A.; SALIM, J. A.; MORAES, F. R.; JARDINE, J. G.; NESHICH, I. A. P.; NESHICH, G. |
Afiliação: |
IVAN MAZONI, CNPTIA; LUIZ CÉSAR BORRO, Estagiário/CNPTIA; ADAUTO LUIZ MANCINI, CNPTIA; JOSÉ AUGUSTO SALIM, Estagiário/CNPTIA; FABIO ROGERIO DE MORAES, Bolsista/CNPTIA; JOSE GILBERTO JARDINE, CNPTIA; IZABELLA AGOSTINHO PENA NESHICH, Estagiária/CNPTIA; GORAN NESHICH, CNPTIA. |
Título: |
Comparison between physical chemical and geometrical characteristics of the amino acids present in alpha-helices and beta-sheets. |
Ano de publicação: |
2009 |
Fonte/Imprenta: |
In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. |
Páginas: |
Não pagiando. |
Idioma: |
Inglês |
Notas: |
X-Meeting 2009. |
Conteúdo: |
JSSD is software developed on the Java programming language, to analyze the secondary structure elements of the proteins. This analysis is based on the information about the amino acids physical chemical and geometrical parameters and allows characterize the functional proteins nanoenvironment, where the nucleation of secondary structure elements (alpha-helix, beta-sheets and loops) occurs (composed by initiation, propagation and termination). JSSD uses a database containing 720 different descriptors for each amino acid in any protein deposited in the PDB. Considering that each protein has 2 chains with 300 amino acids each one and there are more than 60000 structures deposited in the PDB, our database has 720 x 2 x 300 x 60,000 = 25,920,000,000 registers approximately. A first experiment was done with 40,710 proteins. We created data marts (extracts from PDB based on strict rules for selecting a particular characteristic) from these structures for the proteins families: all-alpha, all-beta and alpha + beta. Using only the amino acids sequence matching the initial and final position at selected secondary structure element and that has consensus on all three identifiers PDB, DSSP and Stride, the experiment showed that there are 34,095 alpha-helices on the all-alpha protein family; 8,645 beta-sheets on the all-beta protein family and 306,556 alpha-helices and 250,674 beta-sheets on the alpha + beta protein family (both secondary structure element of variable size starting from minimum 5 amino acids). MenosJSSD is software developed on the Java programming language, to analyze the secondary structure elements of the proteins. This analysis is based on the information about the amino acids physical chemical and geometrical parameters and allows characterize the functional proteins nanoenvironment, where the nucleation of secondary structure elements (alpha-helix, beta-sheets and loops) occurs (composed by initiation, propagation and termination). JSSD uses a database containing 720 different descriptors for each amino acid in any protein deposited in the PDB. Considering that each protein has 2 chains with 300 amino acids each one and there are more than 60000 structures deposited in the PDB, our database has 720 x 2 x 300 x 60,000 = 25,920,000,000 registers approximately. A first experiment was done with 40,710 proteins. We created data marts (extracts from PDB based on strict rules for selecting a particular characteristic) from these structures for the proteins families: all-alpha, all-beta and alpha + beta. Using only the amino acids sequence matching the initial and final position at selected secondary structure element and that has consensus on all three identifiers PDB, DSSP and Stride, the experiment showed that there are 34,095 alpha-helices on the all-alpha protein family; 8,645 beta-sheets on the all-beta protein family and 306,556 alpha-helices and 250,674 beta-sheets on the alpha + beta protein family (both secondary structure element of variable size starting from... Mostrar Tudo |
Palavras-Chave: |
Bioinformática; Geometrical amino acids; Sting. |
Thesaurus Nal: |
Bioinformatics; Computer software. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
Marc: |
LEADER 02481nam a2200277 a 4500 001 1576284 005 2020-01-15 008 2009 bl uuuu u00u1 u #d 100 1 $aMAZONI, I. 245 $aComparison between physical chemical and geometrical characteristics of the amino acids present in alpha-helices and beta-sheets.$h[electronic resource] 260 $aIn: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB$c2009 300 $aNão pagiando. 500 $aX-Meeting 2009. 520 $aJSSD is software developed on the Java programming language, to analyze the secondary structure elements of the proteins. This analysis is based on the information about the amino acids physical chemical and geometrical parameters and allows characterize the functional proteins nanoenvironment, where the nucleation of secondary structure elements (alpha-helix, beta-sheets and loops) occurs (composed by initiation, propagation and termination). JSSD uses a database containing 720 different descriptors for each amino acid in any protein deposited in the PDB. Considering that each protein has 2 chains with 300 amino acids each one and there are more than 60000 structures deposited in the PDB, our database has 720 x 2 x 300 x 60,000 = 25,920,000,000 registers approximately. A first experiment was done with 40,710 proteins. We created data marts (extracts from PDB based on strict rules for selecting a particular characteristic) from these structures for the proteins families: all-alpha, all-beta and alpha + beta. Using only the amino acids sequence matching the initial and final position at selected secondary structure element and that has consensus on all three identifiers PDB, DSSP and Stride, the experiment showed that there are 34,095 alpha-helices on the all-alpha protein family; 8,645 beta-sheets on the all-beta protein family and 306,556 alpha-helices and 250,674 beta-sheets on the alpha + beta protein family (both secondary structure element of variable size starting from minimum 5 amino acids). 650 $aBioinformatics 650 $aComputer software 653 $aBioinformática 653 $aGeometrical amino acids 653 $aSting 700 1 $aBORRO, L. C. 700 1 $aMANCINI, A. 700 1 $aSALIM, J. A. 700 1 $aMORAES, F. R. 700 1 $aJARDINE, J. G. 700 1 $aNESHICH, I. A. P. 700 1 $aNESHICH, G.
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Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
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Biblioteca(s): |
Embrapa Agrobiologia. |
Data corrente: |
29/04/2019 |
Data da última atualização: |
08/11/2019 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 2 |
Autoria: |
SANTOS, T. A. dos; RESENDE, A. S. de; SILVA, F. F. da; MACHADO, A. F. L.; CHAER, G. M. |
Afiliação: |
ALEXANDER SILVA DE RESENDE, CNPAB; FELIPE FERREIRA DA SILVA, UFRJ; UFRRJ; GUILHERME MONTANDON CHAER, CNPAB. |
Título: |
Weed interference factor that affect the growth on an Atlantic Forest tree species. |
Título original: |
Fatores da mato interferência determinantes no crescimento de espécie arbórea da Mata Atlântica |
Ano de publicação: |
2019 |
Fonte/Imprenta: |
Bioscience Journal, v. 35, n. 2, p. 485-494, mar./apr. 2019. |
DOI: |
10.14393/BJ-v35n2a2019-41820 |
Idioma: |
Inglês |
Thesaurus NAL: |
Reforestation; Schinus terebinthifolia; Urochloa brizantha; Weeds. |
Categoria do assunto: |
K Ciência Florestal e Produtos de Origem Vegetal |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/196698/1/Weed-interference-factors.pdf
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Marc: |
LEADER 00799naa a2200229 a 4500 001 2108555 005 2019-11-08 008 2019 bl uuuu u00u1 u #d 024 7 $a10.14393/BJ-v35n2a2019-41820$2DOI 100 1 $aSANTOS, T. A. dos 240 $aFatores da mato interferência determinantes no crescimento de espécie arbórea da Mata Atlântica 245 $aWeed interference factor that affect the growth on an Atlantic Forest tree species.$h[electronic resource] 260 $c2019 650 $aReforestation 650 $aSchinus terebinthifolia 650 $aUrochloa brizantha 650 $aWeeds 700 1 $aRESENDE, A. S. de 700 1 $aSILVA, F. F. da 700 1 $aMACHADO, A. F. L. 700 1 $aCHAER, G. M. 773 $tBioscience Journal$gv. 35, n. 2, p. 485-494, mar./apr. 2019.
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