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Hydrodynamic Radius Prediction of Intrinsically Disordered Proteins
Author(s) -
Ricard Benjamin,
Tomasso Maria,
Whitten Steven
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.598.7
Subject(s) - intrinsically disordered proteins , polyproline helix , computational biology , chemistry , physics , biophysics , biology , biochemistry , peptide
Intrinsically disordered proteins are proteins that do not show a set three‐dimensional tertiary structure and are usually involved in signal‐transduction and transcription regulation. It is estimated that upwards of 33% of all eukaryotic proteins contain intrinsically disordered domains. It is known that hydrodynamic radius (R h ) of IDPs depends largely on their intrinsic propensity to conform into a polyproline‐II helix. A generalized understanding of the molecular organization of IDPs in response to perturbations is presented here. This model uses polyproline‐II propensities and net charge in order to simulate R h and understand the structural properties of IDPs in terms of discrete changes in a system. Fundamental understanding of protein structures in IDPs may provide an avenue for novel drug design, diagnostics, and treatment. Support or Funding Information Research reported in this poster was supported by the National Institute of General Medical Sciences of the National Institutes of Health under award R15GM115603.