2008
DOI: 10.1021/ja710446s
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Role of Backbone−Solvent Interactions in Determining Conformational Equilibria of Intrinsically Disordered Proteins

Abstract: Intrinsically disordered proteins (IDPs) are functional proteins that do not fold into well-defined three-dimensional structures under physiological conditions. IDP sequences have low hydrophobicity, and hence, recent experiments have focused on quantitative studies of conformational ensembles of archetypal IDP sequences such as polyglutamine and glycine-serine block copolypeptides. Results from these experiments show that, despite the absence of hydrophobic residues, polar IDPs prefer ensembles of collapsed s… Show more

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Cited by 205 publications
(281 citation statements)
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“…For each model, the total solvation free energy in TMAO solution is the most unfavorable solution environment (greatest free energy value), whereas the urea solution is the most favorable (lowest free energy). This is consistent with the notion that urea creates a better solution environment for the peptide backbone, [21][22][23] whereas TMAO is a poorer solvent than water. 19 Components analysis of the total solvation free energy allows for a mechanistic view of the thermodynamic effect of osmolyte solution on the solvation of the peptide backbone.…”
Section: Resultssupporting
confidence: 89%
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“…For each model, the total solvation free energy in TMAO solution is the most unfavorable solution environment (greatest free energy value), whereas the urea solution is the most favorable (lowest free energy). This is consistent with the notion that urea creates a better solution environment for the peptide backbone, [21][22][23] whereas TMAO is a poorer solvent than water. 19 Components analysis of the total solvation free energy allows for a mechanistic view of the thermodynamic effect of osmolyte solution on the solvation of the peptide backbone.…”
Section: Resultssupporting
confidence: 89%
“…In the literature, we find a scatter of results from different models. Some previous simulations show urea hydrogen bonding with the peptide carbonyl group, 22,44,45 whereas others see more significant hydrogen bonding with the peptide amides as opposed to the peptide carbonyl group. 46 To provide a further description of the nature of osmolyte and backbone correlations, we have calculated the solvent density profile around the peptide.…”
Section: Resultsmentioning
confidence: 90%
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