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...
主要な著者: | , , , , , |
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フォーマット: | Journal article |
言語: | English |
出版事項: |
National Academy of Sciences
2010
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Quaternary dynamics and plasticity underlie small heat shock protein chaperone function.
出版事項 2010
Journal article