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Protein folding and quinary interactions: creating cellular organisation through functional disorder
Author(s) -
Ribeiro Sara,
Ebbinghaus Simon,
Marcos João C.
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13211
Subject(s) - quinary , destabilisation , globular protein , protein folding , macromolecular crowding , biophysics , intracellular , folding (dsp implementation) , chemistry , globular cluster , biology , biochemistry , physics , macromolecule , psychology , social psychology , organic chemistry , alloy , electrical engineering , engineering , quantum mechanics , galaxy
The marginal stability of globular proteins in the cell is determined by the balance between excluded volume effect and soft interactions. Quinary interactions are a type of soft interactions involved in intracellular organisation and known to have stabilising or destabilising effects on globular proteins. Recent studies suggest that globular proteins have structural flexibility, exhibiting more than one functional state. Here, we propose that the quinary‐induced destabilisation can be sufficient to produce functional partially unfolded states of globular proteins. The biological relevance of this mechanism is explored, involving intracellular phase separation and regulatory stress response mechanisms.