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Cold stability of intrinsically disordered proteins
Author(s) -
Tantos Agnes,
Friedrich Peter,
Tompa Peter
Publication year - 2009
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 - 10.1016/j.febslet.2008.12.054
Subject(s) - intrinsically disordered proteins , globular protein , denaturation (fissile materials) , calpastatin , biophysics , protein stability , chemistry , protein structure , biochemistry , biology , calpain , nuclear chemistry , enzyme
Contrary to globular proteins, intrinsically disordered proteins (IDPs) lack a folded structure and they do not lose solubility at elevated temperatures. Although this should also be true at low temperatures, cold stability of IDPs has not been addressed in any scientific work so far. As direct characterization of cold‐denaturation is difficult, we approached the problem through a freezing‐induced loss‐of‐function model of globular‐disordered functional protein pairs (m‐calpain‐calpastatin, tubulin‐Map2c, Hsp90‐ERD14). Our results affirm that in contrast with globular proteins IDPs are resistant to cold treatment. The theoretical and functional aspects of this observation are discussed.