Abstract
Intrinsically disordered proteins (IDPs) or regions (IDRs) in proteins hold many functions but their biological roles are still not fully understood. Here we describe a new role of such regions. Using the HIV-1 Rev protein, we show that disordered domains have a role in maintaining the correct oligomeric state and the thermodynamic stability of proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 10797-10800 |
| Number of pages | 4 |
| Journal | Chemical Communications |
| Volume | 50 |
| Issue number | 74 |
| DOIs | |
| State | Published - 18 Aug 2014 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
All Science Journal Classification (ASJC) codes
- Electronic, Optical and Magnetic Materials
- Catalysis
- Ceramics and Composites
- General Chemistry
- Surfaces, Coatings and Films
- Metals and Alloys
- Materials Chemistry
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