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. Author manuscript; available in PMC: 2010 Nov 2.
Published in final edited form as: Methods Enzymol. 2009;455:95–125. doi: 10.1016/S0076-6879(08)04204-3

Figure 2. A nearest-neighbor thermodynamic description of repeat-protein stability.

Figure 2

The first two lines (A, B) show single-repeat steps in folding (individual folded repeats are shown as blocks), whereas the last two lines (C, D) show overall folding reactions the fully denatured to the fully native state. Green repeats depict identical sequences, such as consensus repeats, the red and blue repeats represent N- and C-terminal caps.