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...

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Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς:	Stengel, F, Baldwin, A, Painter, A, Robinson, C, Benesch, J, al., E
Μορφή:	Journal article
Γλώσσα:	English
Έκδοση:	National Academy of Sciences 2010

Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. ανά Stengel, F, Baldwin, A, Painter, A, Jaya, N, Basha, E, Kay, L, Vierling, E, Robinson, C, Benesch, J

Έκδοση 2010

Journal article

Quaternary dynamics and plasticity underlie small heat shock protein chaperone function

Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. ανά Stengel, F, Baldwin, A, Painter, A, Jaya, N, Basha, E, Kay, L, Vierling, E, Robinson, C, Benesch, J

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