Molecular chaperones are a group of proteins that bind transiently to nascent polypeptide chains and are thought to function by preventing aggregation by maintaining polypeptides in conformations competent for folding and subunit assembly. On the other hand, specific chaperones are considered to be involved in the mechanism of prion propagation and others are found to colocalize in plaques of patients suffering from neurodegenerative diseases. Solution-state NMR spectroscopy can provide insight into the interactions between the misfolding protein and the chaperone at atomic resolution. In particular, experimental results for Sup35, a yeast prion protein, and β-amyloid, which is responsible for Alzheimer's disease, and their interactions with Hsp104 and αB-crystallin, respectively, are discussed.
