Fig. 5: Proposed mechanism of temperature-induced unfolding and transitioning from reversible to irreversible lysozyme fibrils. | Nature Communications

Fig. 5: Proposed mechanism of temperature-induced unfolding and transitioning from reversible to irreversible lysozyme fibrils.

From: A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein

Fig. 5

The sub-domain B (purple) of the native fold is the first region to denature upon heating and can form the core of the reversible fibrils upon cooling. Longer heating time leads to a full denaturation of the protein, allowing the sub-domain A residues (green) to adopt the beta structure required for the formation of the irreversible fibrils.

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