Investigating how chaperones (don't) work together (IMAGE)
Caption
Solid-state NMR spectroscopy (top right) highlights how DnaJB8 chaperone protein blocks itself. In the displayed NMR data each signal comes from an amino acid in a key part of the chaperone protein: its J-domain. Based on the shape and steepness of the contour lines, we know that this domain is trapped by the chaperone itself, keeping it from doing its job. Fortunately it is also shown how this inactivated state can be disrupted, revealing an intricate orchestration in how chaperone proteins work together to fight and prevent diseases such as Huntington's disease.
Credit
Patrick van der Wel, University of Groningen
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