Title | Cold stability of intrinsically disordered proteins. |
Publication Type | Journal Article |
Year of Publication | 2009 |
Authors | Tantos, Á., P. Friedrich, and P. Tompa |
Journal | FEBS Lett |
Volume | 583 |
Issue | 2 |
Pagination | 465-9 |
Date Published | 2009 Jan 22 |
Type of Article | idp |
ISSN | 1873-3468 |
Keywords | Animals, 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. |
DOI | 10.1016/j.febslet.2008.12.054 |
Alternate Journal | FEBS Lett. |
PubMed ID | 19121309 |
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