A social distancing measure governing the whole proteome
| Autor: | Baik Lin Seong, Seong Il Choi |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0303 health sciences
Protein Folding Proteome Chemistry Macromolecular Substances Physical Distancing Context (language use) Folding (chemistry) 03 medical and health sciences 0302 clinical medicine Structural Biology Excluded volume Biophysics Protein folding Chaperone activity Molecular Biology 030217 neurology & neurosurgery 030304 developmental biology Molecular Chaperones |
| Zdroj: | Current opinion in structural biology. 66 |
| ISSN: | 1879-033X |
| Popis: | Protein folding in vivo has been largely understood in the context of molecular chaperones preventing aggregation of nascent polypeptides in the crowded cellular environment. Nascent chains utilize the crowded environment in favor of productive folding by direct physical connection with cellular macromolecules. The intermolecular repulsive forces by large excluded volume and surface charges of interacting cellular macromolecules, exerting 'social distancing' measure among folding intermediates, could play an important role in stabilizing their physically connected polypeptides against aggregation regardless of the physical connection types. The generic intrinsic chaperone activity of cellular macromolecules likely provides a robust cellular environment for the productive protein folding and solubility maintenance at the whole proteome level. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect