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dc.contributor.author
Lin, Yi Jan  
dc.contributor.author
Schmidt, Andreas  
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Burgardt, Noelia Ines  
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Thiele, Alexandra  
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Weiwad, Matthias  
dc.contributor.author
Lücke, Christian  
dc.date.available
2017-06-13T16:52:33Z  
dc.date.issued
2013-10  
dc.identifier.citation
Lin, Yi Jan; Schmidt, Andreas; Burgardt, Noelia Ines; Thiele, Alexandra; Weiwad, Matthias; et al.; 1H, 13C and 15N resonance assignments of human parvulin 17; Springer; Biomolecular Nmr Assignments; 7; 2; 10-2013; 325-329  
dc.identifier.issn
1874-2718  
dc.identifier.uri
http://hdl.handle.net/11336/18092  
dc.description.abstract
A 25-residue elongation at the N-terminus endows parvulin 17 (Par17) with altered functional properties compared to parvulin 14 (Par14), such as an enhanced influence on microtubule assembly. Therefore the three-dimensional structure of this N-terminal elongation is of particular interest. Here, we report the nearly complete 1H, 13C and 15N chemical shift assignments of Par17. Subsequent chemical shift index analysis indicated that Par17 features a parvulin-type PPIase domain at the C-terminus, analogous to Par14, and an unstructured N-terminus encompassing the first 60 residues. Hence the N-terminus of Par17 apparently adopts a functionally-relevant structure only in presence of the respective interaction partner(s).  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Springer  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Ppiase  
dc.subject
Par14  
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Par17  
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Dna Binding  
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Microtubule Assembly  
dc.subject.classification
Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
1H, 13C and 15N resonance assignments of human parvulin 17  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2017-06-09T15:02:27Z  
dc.identifier.eissn
1874-270X  
dc.journal.volume
7  
dc.journal.number
2  
dc.journal.pagination
325-329  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Dordrecht  
dc.description.fil
Fil: Lin, Yi Jan. Kaohsiung Medical University; China  
dc.description.fil
Fil: Schmidt, Andreas. Max Planck Research Unit for Enzymology of Protein Folding; Alemania  
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Fil: Burgardt, Noelia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Max Planck Research Unit for Enzymology of Protein Folding; Alemania  
dc.description.fil
Fil: Thiele, Alexandra. Max Planck Research Unit for Enzymology of Protein Folding; Alemania  
dc.description.fil
Fil: Weiwad, Matthias. Max Planck Research Unit for Enzymology of Protein Folding; Alemania  
dc.description.fil
Fil: Lücke, Christian. Max Planck Research Unit for Enzymology of Protein Folding; Alemania  
dc.journal.title
Biomolecular Nmr Assignments  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s12104-012-9438-2  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/ark/https://link.springer.com/article/10.1007%2Fs12104-012-9438-2  

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