NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain

The interaction between the acidic transactivation domain of the human tumor suppressor protein p53 (p53TAD) and the 70 kDa subunit of human replication protein A (hRPA70) was investigated using heteronuclear magnetic resonance spectroscopy. A (1)H–(15)N heteronuclear single quantum coherence (HSQC)...

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Detalles Bibliográficos
Autores principales: Vise, Pamela D., Baral, Bharat, Latos, Andrew J., Daughdrill, Gary W.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2005
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1075921/
https://www.ncbi.nlm.nih.gov/pubmed/15824059
http://dx.doi.org/10.1093/nar/gki336

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1075921/
https://www.ncbi.nlm.nih.gov/pubmed/15824059
http://dx.doi.org/10.1093/nar/gki336

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