Hydrodynamic Radii of Intrinsically Disordered Proteins Determined From Experimental Polyproline II Propensities

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dc.contributor.authorTomasso, Maria E.
dc.contributor.authorTarver, Michael J.
dc.contributor.authorDevarajan, Deepa
dc.contributor.authorWhitten, Steven T.
dc.date.accessioned2020-05-26T16:33:54Z
dc.date.available2020-05-26T16:33:54Z
dc.date.issued2016-01
dc.description.abstractThe properties of disordered proteins are thought to depend on intrinsic conformational propensities for polyproline II (PPII) structure. While intrinsic PPII propensities have been measured for the common biological amino acids in short peptides, the ability of these experimentally determined propensities to quantitatively reproduce structural behavior in intrinsically disordered proteins (IDPs) has not been established. Presented here are results from molecular simulations of disordered proteins showing that the hydrodynamic radius (Rh) can be predicted from experimental PPII propensities with good agreement, even when charge-based considerations are omitted. The simulations demonstrate that Rh and chain propensity for PPII structure are linked via a simple power-law scaling relationship, which was tested using the experimental Rh of 22 IDPs covering a wide range of peptide lengths, net charge, and sequence composition. Charge effects on Rh were found to be generally weak when compared to PPII effects on Rh. Results from this study indicate that the hydrodynamic dimensions of IDPs are evidence of considerable sequence-dependent backbone propensities for PPII structure that qualitatively, if not quantitatively, match conformational propensities measured in peptides.
dc.description.departmentChemistry and Biochemistry
dc.formatText
dc.format.extent22 pages
dc.format.medium1 file (.pdf)
dc.identifier.citationTomasso, M. E., Tarver, M. J., Devarajan, D., & Whitten, S. T. (2016). Hydrodynamic radii of intrinsically disordered proteins determined from experimental polyproline II propensities. PLoS Computational Biology, 12(1).
dc.identifier.doihttps://doi.org/10.1371/journal.pcbi.1004686
dc.identifier.issn1553-734X
dc.identifier.urihttps://hdl.handle.net/10877/10312
dc.language.isoen
dc.publisherPublic Library of Science
dc.rights.holder© 2016 Tomasso et al.
dc.rights.licenseThis work is licensed under a Creative Commons Attribution 4.0 International License.
dc.sourcePLoS Computational Biology, 2016, Vol. 12, No. 1, Article e1004686.
dc.subjectpolyproline II
dc.subjectintrinsically disordered proteins
dc.subjecthydrodynamic radii
dc.subjectChemistry and Biochemistry
dc.titleHydrodynamic Radii of Intrinsically Disordered Proteins Determined From Experimental Polyproline II Propensities
dc.typeArticle

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