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- W2009443766 abstract "Synthesis of various independent observations suggests that IDPs can be classified as globule vs. coil formers based on their net charge per residue. Closer scrutiny of the resultant classifications reveals considerable complexity and conformational richness that is masked by considerations of amino acid composition alone. I will present results from our recent work on polyampholytic IDPs, which show that conformational properties of at least a third of naturally occurring IDPs are governed by the linear sequence distribution of oppositely charged residues. This has implications for de novo design of sequence-ensemble relationships as a tool for modulating functions of IDPs. Preliminary results highlighting the utility of sequence design to afford tunability of IDP functions will be discussed. Finally, I will close with a discussion of recent advances that are allowing us to probe how being in cis to ordered domains modulates the sequence-encoded conformational properties of intrinsically disordered regions." @default.
- W2009443766 created "2016-06-24" @default.
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- W2009443766 date "2014-01-01" @default.
- W2009443766 modified "2023-10-14" @default.
- W2009443766 title "Decoding Sequence-Ensemble Relationships of IDPS" @default.
- W2009443766 doi "https://doi.org/10.1016/j.bpj.2013.11.063" @default.
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