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Multiscale Ensemble Modeling of Intrinsically Disordered Proteins: p53 N-Terminal Domain - PMC

ncbi.nlm.nih.gov · 8,678 words · saved by 1 readers

The .gov means it’s official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site. The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely. Intrinsically disordered proteins (IDPs) are ubiquitous and play key roles in transcriptional regulations and other cellular processes. To characterize diverse structural ensembles of IDPs, combinations of NMR and computational modeling showed some promise, but they need further improvements. Here, for accurate and efficient modeling of IDPs, we propose a systematic multiscale computational method. We first perform all-atom replica-exchange molecular dynamics (MD) simulations of a few fragments selected from a target IDP. These results together wit

Biophys J . 2011 Sep 21;101(6):1450–1458. doi: 10.1016/j.bpj.2011.08.003 Multiscale Ensemble Modeling of Intrinsically Disordered Proteins: p53 N-Terminal Domain Tsuyoshi Terakawa Tsuyoshi Terakawa 1 Department of Biophysics Graduate School of Science, Kyoto University, Kyoto, Japan; and CREST Japan Science and Technology Agency, Tokyo, Japan Find articles by Tsuyoshi Terakawa 1 , Shoji Takada Shoji Takada 1 Department of Biophysics Graduate School of Science, Kyoto University, Kyoto, Japan; and CREST Japan Science and Technology Agency, Tokyo, Japan Find articles by Shoji Takada 1, ∗ Author i

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