Figure 1: Comparative analysis of the thermal denaturation for polyubiquitin chains of different length. | Nature Communications

Figure 1: Comparative analysis of the thermal denaturation for polyubiquitin chains of different length.

From: The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates

Figure 1

Differential scanning calorimetry traces of monoubiquitin and linear polyubiquitin chains (a), K63-linked polyubiquitin chains (b) and K48-linked polyubiquitin chains (c) with up to six ubiquitin units. (d) Transition temperatures are plotted against chain length for K48-linked, K63-linked and linear ubiquitin chains. (*In the thermal denaturation of K48-linked hexaubiquitin, the higher transition temperature is selected.).

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