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...

Szczegółowa specyfikacja

Opis bibliograficzny
Główni autorzy:	Stengel, F, Baldwin, A, Painter, A, Robinson, C, Benesch, J, al., E
Format:	Journal article
Język:	English
Wydane:	National Academy of Sciences 2010

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

Wydane 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. od Stengel, F, Baldwin, A, Painter, A, Jaya, N, Basha, E, Kay, L, Vierling, E, Robinson, C, Benesch, J

Podobne zapisy