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Registro Completo
Biblioteca(s): |
Embrapa Agricultura Digital. |
Data corrente: |
04/08/2005 |
Data da última atualização: |
17/01/2020 |
Autoria: |
MANCINI, A. L.; HIGA, R. H.; OLIVEIRA, A.; DOMINIQUINI, F.; FALCAO, P. R. K.; YAMAGISHI, M. E. B.; TOGAWA, R. C.; NESHICH, G. |
Afiliação: |
ADAUTO LUIZ MANCINI, CNPTIA; ROBERTO HIROSHI HIGA, CNPTIA; Cenargen; CNPTIA; PAULA REGINA KUSER FALCAO, CNPTIA; MICHEL EDUARDO BELEZA YAMAGISHI, CNPTIA; ROBERTO COITI TOGAWA, Cenargen; GORAN NESIC, CNPTIA. |
Título: |
Sting contacts: a web-based application for identification and analysis of amino acid contacts within protein structure and across protein interfaces. |
Ano de publicação: |
2004 |
Fonte/Imprenta: |
Bioinformatics, v. 20, n. 13, p. 2145-2147, 2004. |
DOI: |
10.1093/bioinformatics/bth203 |
Idioma: |
Inglês |
Notas: |
Na publicação: P. R. Kuser. |
Conteúdo: |
Amino acid contacts in terms of atomic interactions are essential factors to be considered in the analysis of the structure of a protein and its complexes. Consequently, molecular biologists do require specific tools for the identification and visualization of all such contacts. Graphical contacts (GC) and interface forming residue graphical contacts (IFRgc) presented here, calculate atomic contacts among amino acids based on a table of predefined pairs of the atom types and their distances, and then display them using number of different forms. The inventory of currently listed contact types by GC and IFRgc include hydrogen bonds (in nine different flavors), hydrophobic interactions, charge?charge interactions, aromatic stacking and disulfide bonds. Such extensive catalog of the interactions, representing the forces that govern protein folding, stability and binding, is the key feature of these two applications. GC and IFRgc are part of STING Millennium Suite. |
Palavras-Chave: |
Sting Millennium Suite. |
Thesagro: |
Aminoácido; Proteina. |
Thesaurus NAL: |
Amino acids; Proteins. |
Categoria do assunto: |
-- |
Marc: |
LEADER 01880naa a2200289 a 4500 001 1009086 005 2020-01-17 008 2004 bl uuuu u00u1 u #d 024 7 $a10.1093/bioinformatics/bth203$2DOI 100 1 $aMANCINI, A. L. 245 $aSting contacts$ba web-based application for identification and analysis of amino acid contacts within protein structure and across protein interfaces.$h[electronic resource] 260 $c2004 500 $aNa publicação: P. R. Kuser. 520 $aAmino acid contacts in terms of atomic interactions are essential factors to be considered in the analysis of the structure of a protein and its complexes. Consequently, molecular biologists do require specific tools for the identification and visualization of all such contacts. Graphical contacts (GC) and interface forming residue graphical contacts (IFRgc) presented here, calculate atomic contacts among amino acids based on a table of predefined pairs of the atom types and their distances, and then display them using number of different forms. The inventory of currently listed contact types by GC and IFRgc include hydrogen bonds (in nine different flavors), hydrophobic interactions, charge?charge interactions, aromatic stacking and disulfide bonds. Such extensive catalog of the interactions, representing the forces that govern protein folding, stability and binding, is the key feature of these two applications. GC and IFRgc are part of STING Millennium Suite. 650 $aAmino acids 650 $aProteins 650 $aAminoácido 650 $aProteina 653 $aSting Millennium Suite 700 1 $aHIGA, R. H. 700 1 $aOLIVEIRA, A. 700 1 $aDOMINIQUINI, F. 700 1 $aFALCAO, P. R. K. 700 1 $aYAMAGISHI, M. E. B. 700 1 $aTOGAWA, R. C. 700 1 $aNESHICH, G. 773 $tBioinformatics$gv. 20, n. 13, p. 2145-2147, 2004.
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