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...
| Principais autores: | , , , , , |
|---|---|
| Formato: | Journal article |
| Idioma: | English |
| Publicado em: |
National Academy of Sciences
2010
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Quaternary dynamics and plasticity underlie small heat shock protein chaperone function.
Publicado em 2010
Journal article