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As their name implies, natively disordered proteins (aka, intrinsically unfolded proteins) challenge our very concept of structural biology [6].
Modeling the structure of natively disordered peptides has proved difficult due to the lack of structural information on these peptides.
To explain the conversion of proteins from soluble to fibrous forms, several types of models have been proposed: refolding, natively disordered and gain of interaction.
In this work, we use a novel application of the host-guest method, combining folding theory with experiments, to model the structure of natively disordered polyglutamine peptides.
This natively disordered kinetic trap, interpreted as a molten globule, has a wide temperature range of metastability, and it is identified as the "slow intermediate state" observed in kinetic experiments.
We also found that incorporating natively disordered regions predicted by DISOPRED improves the prediction performance further even further.
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The sentence mentioning that Ump1 is a natively-disordered protein refers to papers from 2008.
Natively-disordered proteins also qualify as proteasome substrates and are cleaved without post-translational ubiquitin modification (Fishbain et al., 2015).
Ump1 is a natively-disordered protein, which is buried inside the pre-holo CP and later on becoming the first substrate of the nascent CP (Kusmierczyk et al., 2008; Ramos & Dohmen, 2008).
In the third paragraph of the Introduction: "Natively-disordered proteins also qualify as proteasome substrates and are cleaved without post-translational ubiquitin modification"., the reference which follows is about something quite different and another more relevant reference should be used.
Furthermore, we included other global sequence information in the form of twenty amino acid compositions, the percentage of three predicted secondary structures, the percentage of predicted exposed/buried residues, and the percentage of natively disordered/ordered residues as well.
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