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< dc:title > 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen </ dc:title >
< dc:creator > Serrano, Soraya </ dc:creator >
< dc:creator > Callís Figueres, Mariona </ dc:creator >
< dc:creator > Vilanova i Brugués, Maria </ dc:creator >
< dc:creator > Benito i Mundet, Antoni </ dc:creator >
< dc:creator > Laurents, Douglas V. </ dc:creator >
< dc:creator > Ribó i Panosa, Marc </ dc:creator >
< dc:creator > Bruix, Marta </ dc:creator >
< dc:contributor > Ministerio de Ciencia e Innovación (Espanya) </ dc:contributor >
< dc:subject > Enginyeria de proteïnes </ dc:subject >
< dc:subject > Protein engineering </ dc:subject >
< dc:subject > Enzims </ dc:subject >
< dc:subject > Enzymes </ dc:subject >
< dc:description > Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35 C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase ® is conserved in the FL-G zymogen </ dc:description >
< dc:description > This work was supported by the projects, CTQ2008-0080, CTQ2010-21567-C02-02 and BFU2009-06935/ BMC from MICINN and PUG2008A from the Universitat de Girona </ dc:description >
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< dc:source > © Biomolecular NMR Assignments, 2013, vol. 7, p. 13-15 </ dc:source >
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< dc:title > 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen </ dc:title >
< dc:creator > Serrano, Soraya </ dc:creator >
< dc:creator > Callís Figueres, Mariona </ dc:creator >
< dc:creator > Vilanova i Brugués, Maria </ dc:creator >
< dc:creator > Benito i Mundet, Antoni </ dc:creator >
< dc:creator > Laurents, Douglas V. </ dc:creator >
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< dc:description > Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35 C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase ® is conserved in the FL-G zymogen </ dc:description >
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< dc:description > Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35 C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase ® is conserved in the FL-G zymogen </ dc:description >
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< creator > Callís Figueres, Mariona </ creator >
< creator > Vilanova i Brugués, Maria </ creator >
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< dc:title > 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen </ dc:title >
< dc:creator > Serrano, Soraya </ dc:creator >
< dc:creator > Callís Figueres, Mariona </ dc:creator >
< dc:creator > Vilanova i Brugués, Maria </ dc:creator >
< dc:creator > Benito i Mundet, Antoni </ dc:creator >
< dc:creator > Laurents, Douglas V. </ dc:creator >
< dc:creator > Ribó i Panosa, Marc </ dc:creator >
< dc:creator > Bruix, Marta </ dc:creator >
< dc:contributor > Ministerio de Ciencia e Innovación (Espanya) </ dc:contributor >
< dc:subject > Enginyeria de proteïnes </ dc:subject >
< dc:subject > Protein engineering </ dc:subject >
< dc:subject > Enzims </ dc:subject >
< dc:subject > Enzymes </ dc:subject >
< dc:description > Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35 C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase ® is conserved in the FL-G zymogen </ dc:description >
< dc:date > 2016-01-28T06:51:58Z </ dc:date >
< dc:date > 2016-01-28T06:51:58Z </ dc:date >
< dc:date > 2013 </ dc:date >
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< dc:identifier > 1874-2718 </ dc:identifier >
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< dc:identifier > 017120 </ dc:identifier >
< dc:identifier > 1874-270X </ dc:identifier >
< dc:language > eng </ dc:language >
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< dc:relation > © Biomolecular NMR Assignments, 2013, vol. 7, p. 13-15 </ dc:relation >
< dc:relation > Articles publicats (D-B) </ dc:relation >
< dc:relation > Bases Moleculares Del Plegamiento Y Citotoxicidad De Las Ribonucleasas Pancreaticas. Evaluacion De La Actividad Citotoxica Y Diseño De Estrategias Para Su Control Mediante Splicing Proteico. </ dc:relation >
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< field name =" value " > Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35 C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase ® is conserved in the FL-G zymogen </ field >
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