2014
DOI: 10.1002/prot.24692
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Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins

Abstract: Molecular transduction of biological signals is understood primarily in terms of the cooperative structural transitions of protein macromolecules, providing a mechanism through which discrete local structure perturbations affect global macromolecular properties. The recognition that proteins lacking tertiary stability, commonly referred to as intrinsically disordered proteins, mediate key signaling pathways suggests that protein structures without cooperative intramolecular interactions may also have the abili… Show more

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Cited by 29 publications
(71 citation statements)
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References 87 publications
(172 reference statements)
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“…The black triangles show molar residue ellipticity at 222 nm at each temperature, corresponding to PPII content. The CD data suggests a small temperature-dependent decrease of PPII content, but this does not translate to the R h as much as would be expected based on previous observations in the literature [51, 52]. As an example, the temperature dependence of the R h of p53(1-93) is shown in gray circles , which also mirrored its own molar residue ellipticity at 221 nm, the local PPII maximum observed for p53 (re-plotted from [51]).…”
Section: Figurecontrasting
confidence: 47%
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“…The black triangles show molar residue ellipticity at 222 nm at each temperature, corresponding to PPII content. The CD data suggests a small temperature-dependent decrease of PPII content, but this does not translate to the R h as much as would be expected based on previous observations in the literature [51, 52]. As an example, the temperature dependence of the R h of p53(1-93) is shown in gray circles , which also mirrored its own molar residue ellipticity at 221 nm, the local PPII maximum observed for p53 (re-plotted from [51]).…”
Section: Figurecontrasting
confidence: 47%
“…A series of well-characterized globular proteins were run over a G-100 Sephadex column to determine the linear relationship between the thermodynamic retention factor ( K D ) and R h for control proteins with known crystal structures [51, 52] (Fig. 2a).…”
Section: Resultsmentioning
confidence: 99%
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“…In this case, the experiments were performed with unlabeled protein at concentrations of denaturant between 0.2 and 6.95 M GdmCl and between 0.58 and 9.02 M urea. The method uses the correlation times of scattering intensity fluctuations to determine molecular translational diffusion coefficients, and hence R h 61 , and is sensitive to small variations in this parameter 75 . Effects from the nonideality of the solution due to the high protein concentrations required were investigated systematically by measurements at different protein concentrations (see SI Text and Figure S9a,b).…”
Section: Resultsmentioning
confidence: 99%
“…Intrinsically disordered proteins represent a comparatively new paradigm in understanding protein structure and the suggestion is that many proteins exist without a defined secondary or tertiary structure as a basis of their molecular function (Dunker et al, 2001). Protein functions thought to depend on intrinsic disorder include flexible linker domains and phosphorylation sites (Dunker et al, 2001;Perez et al, 2014). Given that CD24 is heavily glycosylated in its mature form, it is also plausible that this disorder gives the mature protein additional flexibility to maximize its glycosylation potential through minimizing steric interactions.…”
Section: Discussionmentioning
confidence: 98%