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Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain.

The p53 tumor suppressor oligomerization domain, a dimer of two primary dimers, is an independently folding domain whose subunits consist of a beta-strand, a tight turn and an alpha-helix. To evaluate the effect of hydrophobic side-chains on three-dimensional structure, we substituted residues Phe34...

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Main Authors: McCoy, M, Stavridi, E S, Waterman, J L, Wieczorek, A M, Opella, S J, Halazonetis, T D
Formato: Artigo
Idioma:Inglês
Publicado: 1997
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC1326307/
https://ncbi.nlm.nih.gov/pubmed/9321402
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/16.20.6230
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