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. 2006 Dec 27;109(8):3538–3543. doi: 10.1182/blood-2006-07-038588

Figure 6.

Figure 6

Proline mutation alters folding state. (A) Plot of helicity compared with fraction unlabeled cysteine at temperatures ranging from 20°C to 60°C reveals divergent unfolding pathways on mutation (B) The reduced structural stability of the mutant is speculated to add flexibility and to increase entropy in destabilizing the αβassociation in the tetramer.