Quaternary dynamics and plasticity underlie small heat shock protein chaperone function
Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that prevent protein aggregation by binding clients destabilized during cellular stress. Here we probe the architecture and dynamics of complexes formed between an oligomeric sHSP and client by employing unique mass spect...
| Hoofdauteurs: | , , , , , |
|---|---|
| Formaat: | Journal article |
| Taal: | English |
| Gepubliceerd in: |
National Academy of Sciences
2010
|
Search Result 1
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function.
Gepubliceerd in 2010
Journal article