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- W1973033666 abstract "The disulfide-reduced form of bovine ribonuclease A, with the Cys thiols irreversibly blocked, was characterized by small-angle x-ray scattering. To help resolve the conflicting results and interpretations from previous studies of this model unfolded protein, we measured scattering profiles using a range of solution conditions and compared them with the profiles predicted by a computational model for a random-coil polypeptide. Analysis of the simulated and experimental profiles reveals that scattering intensities at intermediate angles, corresponding to interatomic distances in the range of 5-20 A, are particularly sensitive to changes in solvation and can be used to assess the internal scaling behavior of the polypeptide chain, expressed as a mass fractal dimension, D(m). This region of the scattering curve is also much less sensitive to experimental artifacts than is the very small angle regime (the Guinier region) that has been more typically used to characterize unfolded proteins. The experimental small-angle x-ray scattering profiles closely matched those predicted by the computational model assuming relatively small solvation energies. The scaling behavior of the polypeptide approaches that of a well-solvated polymer under conditions where it has a large net charge and at high urea concentrations. At lower urea concentrations and neutral pH, the behavior of the chain approaches that expected for theta-conditions, where the effects of slightly unfavorable interactions with solvent balance those of excluded volume, leading to scaling behavior comparable to that of an idealized random walk chain. Though detectable, the shift toward more compact conformations at lower urea concentrations does not correspond to a transition to a globule state and is associated with little or no reduction in conformational entropy. This type of collapse, therefore, is unlikely to greatly reduce the conformational search for the native state." @default.
- W1973033666 created "2016-06-24" @default.
- W1973033666 creator A5025867911 @default.
- W1973033666 creator A5032111372 @default.
- W1973033666 creator A5065418938 @default.
- W1973033666 date "2008-04-01" @default.
- W1973033666 modified "2023-10-14" @default.
- W1973033666 title "Small-Angle X-ray Scattering of Reduced Ribonuclease A: Effects of Solution Conditions and Comparisons with a Computational Model of Unfolded Proteins" @default.
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- W1973033666 doi "https://doi.org/10.1016/j.jmb.2008.02.009" @default.
- W1973033666 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2651769" @default.
- W1973033666 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18329044" @default.
- W1973033666 hasPublicationYear "2008" @default.
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