| Range |
~30 %
|
| Organism |
Eukaryotes |
| Reference |
Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU. Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem. 2013 82:323-55. doi: 10.1146/annurev-biochem-060208-092442. p.325 left column top paragraphPubMed ID23746257
|
| Primary Source |
[14] Dunker AK, Silman I, Uversky VN, Sussman, JL. 2008. Function and structure of inherently disordered proteins. Curr. Opin. Struct. Biol. 18: 756–64 doi: 10.1016/j.sbi.2008.10.002.PubMed ID18952168
|
| Comments |
P.324 right column bottom paragraph: "Protein Folding and Aggregation: The folded three-dimensional structures of most proteins represent a compromise between thermodynamic stability and the conformational flexibility required for function. Consequently, proteins are often marginally stable in their physiological environment and thus susceptible to misfolding and aggregation (refs 2, 3). In addition, a substantial fraction of proteins in eukaryotic cells (∼30%) are classified as intrinsically unstructured and contain regions thought to adopt ordered structure only upon interaction with binding partners (primary source). Such proteins may be metastable and prone to aggregation." |
| Entered by |
Uri M |
| ID |
113341 |