Show simple item record

dc.contributor.authorEnglish, Lance R. ( Orcid Icon 0000-0002-1850-7729 )
dc.contributor.authorTilton, Erin C. ( )
dc.contributor.authorRicard, Benjamin J. ( )
dc.contributor.authorWhitten, Steven T. ( )
dc.date.accessioned2020-04-13T15:04:01Z
dc.date.available2020-04-13T15:04:01Z
dc.date.issued2017-02
dc.identifier.citationEnglish, L. R., Tilton, E. C., Ricard, B. J., & Whitten, S. T. (2017). Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins. Proteins, 85(2), pp. 296–311.en_US
dc.identifier.issn0887-3585
dc.identifier.urihttps://digital.library.txstate.edu/handle/10877/9587
dc.description.abstractProteins that lack tertiary stability under normal conditions, known as intrinsically disordered, exhibit a wide range of biological activities. Molecular descriptions for the biology of intrinsically disordered proteins (IDPs) consequently rely on disordered structural models, which in turn require experiments that assess the origins to structural features observed. For example, while hydrodynamic size is mostly insensitive to sequence composition in chemically denatured proteins, IDPs show strong sequence-specific effects in the hydrodynamic radius (Rh ) when measured under normal conditions. To investigate sequence-modulation of IDP Rh , disordered ensembles generated by a hard sphere collision model modified with a structure-based parameterization of the solution energetics were used to parse the contributions of net charge, main chain dihedral angle bias, and excluded volume on hydrodynamic size. Ensembles for polypeptides 10-35 residues in length were then used to establish power-law scaling relationships for comparison to experimental Rh from 26 IDPs. Results showed the expected outcomes of increased hydrodynamic size from increases in excluded volume and net charge, and compaction from chain-solvent interactions. Chain bias representing intrinsic preferences for α helix and polyproline II (PPII ), however, modulated Rh with intricate dependence on the simulated propensities. PPII propensities at levels expected in IDPs correlated with heightened Rh sensitivity to even weak α helix propensities, indicating bias for common (φ, ψ) are important determinants of hydrodynamic size. Moreover, data show that IDP Rh can be predicted from sequence with good accuracy from a small set of physicochemical properties, namely intrinsic conformational propensities and net charge. Proteins 2017; 85:296-311.en_US
dc.formatText
dc.format.extent29 pages
dc.format.medium1 file (.pdf)
dc.language.isoen_USen_US
dc.publisherJohn Wiley & Sons
dc.sourceProteins, 2017, Vol. 85, No. 2, pp. 296–311.
dc.subjectDynamic light scatteringen_US
dc.subjectNet charge
dc.subjectPolyproline type II
dc.subjectSimulation
dc.subjectSize exclusion chromatography
dc.titleIntrinsic α Helix Propensities Compact Hydrodynamic Radii in Intrinsically Disordered Proteinsen_US
txstate.documenttypeArticle
dc.description.versionThis is the accepted manuscript version of an article published in Proteins.
dc.identifier.doihttps://doi.org/10.1002/prot.25222
txstate.departmentChemistry and Biochemistry


Download

Thumbnail

This item appears in the following Collection(s)

Show simple item record