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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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| Hoofdauteurs: | , , , , , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
1997
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| Onderwerpen: | |
| Online toegang: | 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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