Mostrar el registro sencillo del ítem

dc.contributor.author
Lin, Yi Jan
dc.contributor.author
Schmidt, Andreas
dc.contributor.author
Burgardt, Noelia Ines
dc.contributor.author
Thiele, Alexandra
dc.contributor.author
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
dc.subject
Par17
dc.subject
Dna Binding
dc.subject
Microtubule Assembly
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
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
dc.description.fil
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


Archivos asociados

Documento no disponible

Comunidades y colecciones

  • Articulos(IQUIFIB) [343]
    Articulos de INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"

Mostrar el registro sencillo del ítem