Cold stability of intrinsically disordered proteins.
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.
Tantos
Agnes
A
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina út 29, H-1113 Budapest, Hungary.
Friedrich
Peter
P
Tompa
Peter
P
D000818:Animals; D029681:Arabidopsis Proteins / Q000737:chemistry; D002135:Calcium-Binding Proteins / Q000737:chemistry; D002154:Calpain / Q000737:chemistry; D002417:Cattle; D003080:Cold Temperature; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D014404:Tubulin / Q000737:chemistry
D029681:Arabidopsis Proteins; D002135:Calcium-Binding Proteins; C089006:ERD14 protein, Arabidopsis; D018841:HSP90 Heat-Shock Proteins; D008869:Microtubule-Associated Proteins; D014404:Tubulin; C033668:calpastatin; D002154:Calpain; C449000:m-calpain