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Figure 3 | Alzheimer's Research & Therapy

Figure 3

From: On the subject of rigor in the study of amyloid β-protein assembly

Figure 3

Complex folding surface. Schematic free-energy (F) surface representing features of the folding of hen lysozyme (a protein of 129 residues whose structure consists of two domains denoted α and β). Qα and Qβ are the numbers of native contacts in the α and β domains. The yellow trajectory is a ‘fast track’ in which the α and β domains form concurrently and populate the intermediate (labeled α/β) only transiently. The red trajectory is a ‘slow track’ in which the chain becomes trapped in a long-lived intermediate with persistent structure in only the α domain. Further folding requires either a transition over a higher energy barrier or partial unfolding to enable the remainder of the folding process to occur along the fast track. Residues whose amide hydrogens are protected from solvent exchange in the native structure (as assessed by NMR) are colored red (α domain) or yellow (β domain). All others are blue. Adapted from [51].

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