Abstract
A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit (chain / domain). The analysis includes all the Homo Sapiens as well as Mus Musculus proteins present in the DisProt database for which the structure is available. In the analysis, the fuzzy oil drop modified model (FOD-M) was used, taking into account the external force field, modified by the presence of other factors apart from polar water, influencing protein structuring. The paper presents an alternative to secondary-structure-based classification of intrinsically disordered regions (IDR). The basis of our classification is the ordering of hydrophobic core as calculated by the FOD-M model resulting in FOD-ordered or FOD-unordered IDRs.
Funder
Uniwersytet Jagielloński Collegium Medicum
Publisher
Public Library of Science (PLoS)
Reference58 articles.
1. Classification of intrinsically disordered regions and proteins;R Van der Lee;Chem Rev,2014
2. Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview;F Lermyte;Life (Basel),2020
3. Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions;CJ Oldfield;Annual Review of Biochemistry,2014
4. Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions;CJ Oldfield;Annual Review of Biochemistry,2014
5. The triple power of D3: protein intrinsic disorder in degenerative diseases;VN Uversky;Front Biosci (Landmark Ed),2014
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