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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
07/12/2007 |
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Data da última atualização: |
11/05/2017 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
FERNANDEZ, J. H.; MELLO, M. O; GALGARO, L.; TANAKA, A. S.; SILVA-FILHO, M. C.; NESHICH, G. |
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Afiliação: |
LNCC, Petrópolis, RJ; Esalq/USP; Esalq/USP; Unifesp; Esalq/USP; GORAN NESHICH, CNPTIA. |
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Título: |
Proteinase inhibition using small Bowman-Birk-type structures. |
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Ano de publicação: |
2007 |
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Fonte/Imprenta: |
Genetics and Molecular Research, v. 6, n. 4, p. 846-858, 2007. |
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Idioma: |
Inglês |
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Conteúdo: |
Absttract . Bowman-Birk inhibitors (BBIs) are cysteine-rich and highly cross-linked small proteins that function as specific pseudosubstrates for digestive proteinases. They typically display a "double-headed" structure containing an independent proteinase-binding loop that can bind and inhibit trypsin, chymotrypsin and elastase. In the present study, we used computational biology to study the structural characteristics and dynamics of the inhibition mechanism of the small BBI loop expressing a 35-amino acid polypeptide (ChyTB2 inhibitor) which has coding region for the mutated chymotrypsin-inhibitory site of the soybean BBI. We found that in the BBI-trypsin inhibition complex, the most important interactions are salt bridges and hydrogen bonds, whereas in the BBI-chymotrypsin inhibition complex, the most important interactions are hydrophobic. At the same time, ChyTB2 mutant structure maintained the individual functional domain structure and excellent binding/inhibiting capacities for trypsin and chymotrypsin at the same time. These results were confirmed by enzyme-linked immunosorbend assay experiments. The results showed that modeling combined with molecular dynamics is an efficient method to describe, predict and then obtain new proteinase inhibitors. For such study, however, it is necessary to start from the sequence and structure of the mutant interacting relatively strongly with both trypsin and chymotrypsin for designing the small BBI-type inhibitor against proteinases. MenosAbsttract . Bowman-Birk inhibitors (BBIs) are cysteine-rich and highly cross-linked small proteins that function as specific pseudosubstrates for digestive proteinases. They typically display a "double-headed" structure containing an independent proteinase-binding loop that can bind and inhibit trypsin, chymotrypsin and elastase. In the present study, we used computational biology to study the structural characteristics and dynamics of the inhibition mechanism of the small BBI loop expressing a 35-amino acid polypeptide (ChyTB2 inhibitor) which has coding region for the mutated chymotrypsin-inhibitory site of the soybean BBI. We found that in the BBI-trypsin inhibition complex, the most important interactions are salt bridges and hydrogen bonds, whereas in the BBI-chymotrypsin inhibition complex, the most important interactions are hydrophobic. At the same time, ChyTB2 mutant structure maintained the individual functional domain structure and excellent binding/inhibiting capacities for trypsin and chymotrypsin at the same time. These results were confirmed by enzyme-linked immunosorbend assay experiments. The results showed that modeling combined with molecular dynamics is an efficient method to describe, predict and then obtain new proteinase inhibitors. For such study, however, it is necessary to start from the sequence and structure of the mutant interacting relatively strongly with both trypsin and chymotrypsin for designing the small BBI-type inhibitor against proteinas... Mostrar Tudo |
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Palavras-Chave: |
Bioinformática; Enzyme specificity; Inibidor Bowman-Birk; Modelagem molecular; Molecular modeling. |
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Thesagro: |
Proteína. |
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Thesaurus Nal: |
Bioinformatics; Enzyme-linked immunosorbent assay; Models. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/159697/1/AP-Proteinase-GMR-2007.pdf
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Marc: |
LEADER 02330naa a2200289 a 4500
001 1000764
005 2017-05-11
008 2007 bl uuuu u00u1 u #d
100 1 $aFERNANDEZ, J. H.
245 $aProteinase inhibition using small Bowman-Birk-type structures.$h[electronic resource]
260 $c2007
520 $aAbsttract . Bowman-Birk inhibitors (BBIs) are cysteine-rich and highly cross-linked small proteins that function as specific pseudosubstrates for digestive proteinases. They typically display a "double-headed" structure containing an independent proteinase-binding loop that can bind and inhibit trypsin, chymotrypsin and elastase. In the present study, we used computational biology to study the structural characteristics and dynamics of the inhibition mechanism of the small BBI loop expressing a 35-amino acid polypeptide (ChyTB2 inhibitor) which has coding region for the mutated chymotrypsin-inhibitory site of the soybean BBI. We found that in the BBI-trypsin inhibition complex, the most important interactions are salt bridges and hydrogen bonds, whereas in the BBI-chymotrypsin inhibition complex, the most important interactions are hydrophobic. At the same time, ChyTB2 mutant structure maintained the individual functional domain structure and excellent binding/inhibiting capacities for trypsin and chymotrypsin at the same time. These results were confirmed by enzyme-linked immunosorbend assay experiments. The results showed that modeling combined with molecular dynamics is an efficient method to describe, predict and then obtain new proteinase inhibitors. For such study, however, it is necessary to start from the sequence and structure of the mutant interacting relatively strongly with both trypsin and chymotrypsin for designing the small BBI-type inhibitor against proteinases.
650 $aBioinformatics
650 $aEnzyme-linked immunosorbent assay
650 $aModels
650 $aProteína
653 $aBioinformática
653 $aEnzyme specificity
653 $aInibidor Bowman-Birk
653 $aModelagem molecular
653 $aMolecular modeling
700 1 $aMELLO, M. O
700 1 $aGALGARO, L.
700 1 $aTANAKA, A. S.
700 1 $aSILVA-FILHO, M. C.
700 1 $aNESHICH, G.
773 $tGenetics and Molecular Research$gv. 6, n. 4, p. 846-858, 2007.
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Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
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Registro Completo
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Biblioteca(s): |
Embrapa Clima Temperado. |
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Data corrente: |
15/06/2022 |
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Data da última atualização: |
15/06/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
MAYNARD, D. S.; BIALIC-MURPHY, L.; ZOHNER, C. M.; AVERILL, C.; VAN DEN HOOGEN, J.; MA, H.; MO, L.; SMITH, G. R.; ACOSTA, A. T. R.; AUBIN, I.; BERENGUER, E.; BOONMAN, C. C. F.; CATFORD, J. A.; CERABOLINI, B. E. L.; DIAS, A. S.; GONZÁLEZ-MELO, A.; HIETZ, P.; LUSK, C. H.; MORI, A. S.; NIINEMETS, Ü.; PILLAR, V. D.; PINHO, B. X.; ROSELL, J. A.; SCHURR, F. M.; SHEREMETEV, S. N.; SILVA, A. C. da; SOSINSKI JUNIOR, E. E.; VAN BODEGOM, P. M.; WEIHER, E.; BÖNISCH, G.; KATTGE, J.; CROWTHER, T. W. |
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Afiliação: |
DANIEL S. MAYNARD; LALASIA BIALIC-MURPHY; CONSTANTIN M. ZOHNER; COLIN AVERILL; JOHAN VAN DEN HOOGEN; HAOZHI MA; LIDONG MO; GABRIEL REUBEN SMITH; ALICIA T. R. ACOSTA; ISABELLE AUBIN; ERIKA BERENGUER; COLINE C. F. BOONMAN; JANE A. CATFORD; BRUNO E. L. CERABOLINI; ARILDO S. DIAS, Goethe University; ANDRÉS GONZÁLEZ-MELO; PETER HIETZ; CHRISTOPHER H. LUSK; AKIRA S. MORI; ÜLO NIINEMETS; VALÉRIO D. PILLAR; BRUNO X. PINHO; JULIETA A. ROSELL; FRANK M. SCHURR; SERGE N. SHEREMETEV; ANA CAROLINA DA SILVA; ENIO EGON SOSINSKI JUNIOR, CPACT; PETER M. VAN BODEGOM; EVAN WEIHER; GERHARD BÖNISCH; JENS KATTGE; THOMAS W. CROWTHER. |
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Título: |
Global relationships in tree functional traits. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Nature Communications, v. 13, 3185, 2022. |
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Páginas: |
12 p. |
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DOI: |
10.1038 /s41467-022-308 88-2 |
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Idioma: |
Inglês |
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Conteúdo: |
Due to massive energetic investments in woody support structures, trees are subject to unique physiological, mechanical, and ecological pressures not experienced by herbaceous plants. Despite a wealth of studies exploring trait relationships across the entire plant kingdom, the dominant traits underpinning these unique aspects of tree form and function remain unclear. Here, by considering 18 functional traits, encompassing leaf, seed, bark, wood, crown, and root characteristics, we quantify the multidimensional relationships in tree trait expression. We? nd that nearly half of trait variation is captured by two axes: one re? ecting leaf economics, the other re? ecting tree size and competition for light. Yet these orthogonal axes reveal strong environmental convergence, exhibiting correlated responses to temperature, moisture, and elevation. By subsequently exploring multidimensional trait relationships, we show that the full dimensionality of trait space is captured by eight distinct clusters, each re? ecting a unique aspect of tree form and function. Collectively, this work identi? es a core set of traits needed to quantify global patterns in functional biodiversity, and it contributes to our fundamental understanding of the functioning of forests worldwide. |
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Thesagro: |
Árvore; Biodiversidade; Floresta. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1144124/1/2022-Maynard-et-al-Global-relationships-in-tree-functional-traits.pdf
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Marc: |
LEADER 02711naa a2200553 a 4500
001 2144124
005 2022-06-15
008 2022 bl uuuu u00u1 u #d
024 7 $a10.1038 /s41467-022-308 88-2$2DOI
100 1 $aMAYNARD, D. S.
245 $aGlobal relationships in tree functional traits.$h[electronic resource]
260 $c2022
300 $a12 p.
520 $aDue to massive energetic investments in woody support structures, trees are subject to unique physiological, mechanical, and ecological pressures not experienced by herbaceous plants. Despite a wealth of studies exploring trait relationships across the entire plant kingdom, the dominant traits underpinning these unique aspects of tree form and function remain unclear. Here, by considering 18 functional traits, encompassing leaf, seed, bark, wood, crown, and root characteristics, we quantify the multidimensional relationships in tree trait expression. We? nd that nearly half of trait variation is captured by two axes: one re? ecting leaf economics, the other re? ecting tree size and competition for light. Yet these orthogonal axes reveal strong environmental convergence, exhibiting correlated responses to temperature, moisture, and elevation. By subsequently exploring multidimensional trait relationships, we show that the full dimensionality of trait space is captured by eight distinct clusters, each re? ecting a unique aspect of tree form and function. Collectively, this work identi? es a core set of traits needed to quantify global patterns in functional biodiversity, and it contributes to our fundamental understanding of the functioning of forests worldwide.
650 $aÁrvore
650 $aBiodiversidade
650 $aFloresta
700 1 $aBIALIC-MURPHY, L.
700 1 $aZOHNER, C. M.
700 1 $aAVERILL, C.
700 1 $aVAN DEN HOOGEN, J.
700 1 $aMA, H.
700 1 $aMO, L.
700 1 $aSMITH, G. R.
700 1 $aACOSTA, A. T. R.
700 1 $aAUBIN, I.
700 1 $aBERENGUER, E.
700 1 $aBOONMAN, C. C. F.
700 1 $aCATFORD, J. A.
700 1 $aCERABOLINI, B. E. L.
700 1 $aDIAS, A. S.
700 1 $aGONZÁLEZ-MELO, A.
700 1 $aHIETZ, P.
700 1 $aLUSK, C. H.
700 1 $aMORI, A. S.
700 1 $aNIINEMETS, Ü.
700 1 $aPILLAR, V. D.
700 1 $aPINHO, B. X.
700 1 $aROSELL, J. A.
700 1 $aSCHURR, F. M.
700 1 $aSHEREMETEV, S. N.
700 1 $aSILVA, A. C. da
700 1 $aSOSINSKI JUNIOR, E. E.
700 1 $aVAN BODEGOM, P. M.
700 1 $aWEIHER, E.
700 1 $aBÖNISCH, G.
700 1 $aKATTGE, J.
700 1 $aCROWTHER, T. W.
773 $tNature Communications$gv. 13, 3185, 2022.
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