Cold stability of intrinsically disordered proteins.

TitleCold stability of intrinsically disordered proteins.
Publication TypeJournal Article
Year of Publication2009
AuthorsTantos, Á., P. Friedrich, and P. Tompa
JournalFEBS Lett
Volume583
Issue2
Pagination465-9
Date Published2009 Jan 22
Type of Articleidp
ISSN1873-3468
KeywordsAnimals, Arabidopsis Proteins, Calcium-Binding Proteins, Calpain, Cattle, Cold Temperature, HSP90 Heat-Shock Proteins, Humans, Microtubule-Associated Proteins, Protein Denaturation, Protein Folding, Tubulin
Abstract

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.

DOI10.1016/j.febslet.2008.12.054
Alternate JournalFEBS Lett.
PubMed ID19121309