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Domain–domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy

The tumor suppressor p53 is a homotetramer of 4 × 393 residues. Its core domain and tetramerization domain are linked and flanked by intrinsically disordered sequences, which hinder its full structural characterization. There is an outstanding problem of the state of the tetramerization domain. Stru...

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Autors principals: Bista, Michal, Freund, Stefan M., Fersht, Alan R.
Format: Artigo
Idioma:Inglês
Publicat: National Academy of Sciences 2012
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC3465378/
https://ncbi.nlm.nih.gov/pubmed/22972749
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1214176109
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