New insights into disordered proteins and regions according to the FOD-M model

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...

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Bibliographic Details
Published in:PloS one 2022-10, Vol.17 (10), p.e0275300
Main Authors: Roterman, Irena, Stapor, Katarzyna, Fabian, Piotr, Konieczny, Leszek
Format: Article
Language:English
Subjects:
Analysis
Animal models in research
Animals
Biology and Life Sciences
Classification
Evaluation
Humans
Hydrophobic and Hydrophilic Interactions
Hydrophobicity
Intrinsically Disordered Proteins - chemistry
Mice
Polar waters
Protein Conformation
Protein Structure, Secondary
Proteins
Research and Analysis Methods
Water
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0275300