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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
14/11/2024 |
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Data da última atualização: |
25/08/2025 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
MAZONI, I.; SALIM, J. A; MORAES, F. R. de; CORREA, J. L.; BORRO, L. C.; NESHICH, G. |
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Afiliação: |
IVAN MAZONI, CNPTIA; JOSÉ AUGUSTO SALIM, UNIVERSIDADE ESTADUAL DE CAMPINAS; FÁBIO ROGERIO DE MORAES, UNIVERSIDADE ESTADUAL PAULISTA "JÚLIO DE MESQUITA FILHO"; JORGE LUIZ CORREA, CNPTIA; LUIZ CÉSAR BORRO, CLARO BEON; GORAN NESIC, CNPTIA. |
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Título: |
Comprehensive analysis of the distinct nano environments characteristics containing the different secondary structure elements: alpha-helices, beta-sheets, and turns. |
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Ano de publicação: |
2025 |
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Fonte/Imprenta: |
Current Nanomedicine, v. 15, n. 3, p. 267-285, 2025. |
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DOI: |
http://dx.doi.org/10.2174/0124681873291766240724055136 |
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Idioma: |
Inglês |
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Conteúdo: |
This work is the third part of our initiative to fully describe the internal protein nano environments (NEs) for the three existing types of secondary structure elements (SSE). In our previous work, the NE of both the α-helix and the β-sheet were analyzed. The focus of this and previous research is improving our understanding of the SSEs: α-helices, β-sheets and turns, within protein structures. We found that the structural similarities between turns and α-helices are very high and turns may be considered as the “incomplete” initiation of α-helices. The knowledge we were able to compile during this work might be essential for predicting a tertiary structure of proteins, with higher precision and subsequently being in a more favourable position with regard to designing drugs for certain protein structure/function related diseases. Considering that the formation of secondary structure elements is a crucial step in the general folding of protein 3D structure, an important contribution of this work is augmenting the efficiency of estimating if modelled structures, for example, are predicting SSEs in full agreement to necessary/required/sufficient values of respective SSEs nanoenvironment descriptors. During exactly that modelling phase, preceding the more precise final 3D protein structure construction, our Dictionary of Most Relevant Nanoenvironment Descriptors is able to answer some fundamental questions regarding SSE correctness with regard to nanoenvironment characteristics found to be generally required. Expanding this vision, our current work is part of an effort by our laboratory to create a “dictionary of internal protein nanoenvironments” - DIPN. The ten most studied internal protein nanoenvironments are described in DIPN in physicochemical and structural terms, and this knowledge is now available to be used to aid drug design - probably the most important area of application for the results we are presenting here. MenosThis work is the third part of our initiative to fully describe the internal protein nano environments (NEs) for the three existing types of secondary structure elements (SSE). In our previous work, the NE of both the α-helix and the β-sheet were analyzed. The focus of this and previous research is improving our understanding of the SSEs: α-helices, β-sheets and turns, within protein structures. We found that the structural similarities between turns and α-helices are very high and turns may be considered as the “incomplete” initiation of α-helices. The knowledge we were able to compile during this work might be essential for predicting a tertiary structure of proteins, with higher precision and subsequently being in a more favourable position with regard to designing drugs for certain protein structure/function related diseases. Considering that the formation of secondary structure elements is a crucial step in the general folding of protein 3D structure, an important contribution of this work is augmenting the efficiency of estimating if modelled structures, for example, are predicting SSEs in full agreement to necessary/required/sufficient values of respective SSEs nanoenvironment descriptors. During exactly that modelling phase, preceding the more precise final 3D protein structure construction, our Dictionary of Most Relevant Nanoenvironment Descriptors is able to answer some fundamental questions regarding SSE correctness with regard to nanoenvironment characteristics ... Mostrar Tudo |
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Palavras-Chave: |
Aminoácidos; Banco de dados STING; Elementos de estrutura secundária; Nano environments; Nanoambientes; Secondary structure elements; STING´s database. |
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Thesaurus Nal: |
Amino acids; Protein secondary structure. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02985naa a2200301 a 4500
001 2169130
005 2025-08-25
008 2025 bl uuuu u00u1 u #d
024 7 $ahttp://dx.doi.org/10.2174/0124681873291766240724055136$2DOI
100 1 $aMAZONI, I.
245 $aComprehensive analysis of the distinct nano environments characteristics containing the different secondary structure elements$balpha-helices, beta-sheets, and turns.$h[electronic resource]
260 $c2025
520 $aThis work is the third part of our initiative to fully describe the internal protein nano environments (NEs) for the three existing types of secondary structure elements (SSE). In our previous work, the NE of both the α-helix and the β-sheet were analyzed. The focus of this and previous research is improving our understanding of the SSEs: α-helices, β-sheets and turns, within protein structures. We found that the structural similarities between turns and α-helices are very high and turns may be considered as the “incomplete” initiation of α-helices. The knowledge we were able to compile during this work might be essential for predicting a tertiary structure of proteins, with higher precision and subsequently being in a more favourable position with regard to designing drugs for certain protein structure/function related diseases. Considering that the formation of secondary structure elements is a crucial step in the general folding of protein 3D structure, an important contribution of this work is augmenting the efficiency of estimating if modelled structures, for example, are predicting SSEs in full agreement to necessary/required/sufficient values of respective SSEs nanoenvironment descriptors. During exactly that modelling phase, preceding the more precise final 3D protein structure construction, our Dictionary of Most Relevant Nanoenvironment Descriptors is able to answer some fundamental questions regarding SSE correctness with regard to nanoenvironment characteristics found to be generally required. Expanding this vision, our current work is part of an effort by our laboratory to create a “dictionary of internal protein nanoenvironments” - DIPN. The ten most studied internal protein nanoenvironments are described in DIPN in physicochemical and structural terms, and this knowledge is now available to be used to aid drug design - probably the most important area of application for the results we are presenting here.
650 $aAmino acids
650 $aProtein secondary structure
653 $aAminoácidos
653 $aBanco de dados STING
653 $aElementos de estrutura secundária
653 $aNano environments
653 $aNanoambientes
653 $aSecondary structure elements
653 $aSTING´s database
700 1 $aSALIM, J. A
700 1 $aMORAES, F. R. de
700 1 $aCORREA, J. L.
700 1 $aBORRO, L. C.
700 1 $aNESHICH, G.
773 $tCurrent Nanomedicine$gv. 15, n. 3, p. 267-285, 2025.
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| 1. |  | CURRENT, D.; ROSSI, L. M. B.; SABOGAL, C.; NALVARTE, W. Comparación del potencial del manejo de la regeneración natural con asocio agroforestal y plantaciones puras para tres especies: estudio de caso en Brasil, Perú y Costa Rica. In: CONGRESO LATINOAMERICANO IUFRO, 1., 1998, Valdivia, Chile. El manejo sustentable de los recursos forestales, desafio del siglo XXI: actas. [S.l.]: CONAF: IUFRO, 1998.| Tipo: Artigo em Anais de Congresso |
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| 2. | | CURRENT, D. A.; SMITH, J.; SABOGAL, C.; FINEGAN, B.; SÁ, T. D. de A.; MEJIA, A.; NALVARTE, W.; DIAZ, A. Managing fallows for the generation of products and services from woods biomass: an emerging option for resource poor farmers on the agriculturae frontier in tropical América. In: ANNUAL MEETINGS, 2000, Minneapolis. Abstracts. Madison: ASA: CSSA: SSSA, 2000. p. 65.| Tipo: Resumo em Anais de Congresso |
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