. Author manuscript; available in PMC: 2009 Jan 1.

Published in final edited form as: Arch Biochem Biophys. 2007 Sep 15;469(1):83–99. doi: 10.1016/j.abb.2007.08.034

Table 3.

Intrinsic and interfacial free energies from Ising analysis of repeat-protein folding

	ΔG°_intrinsic (kcal/mol)	ΔG°_interface (kcal/mol)
Notch ankyrin	+6.6	−9.1
Consensus TPR	+2.3 (per helix)	−4.5

ΔG° values for the Notch ankyrin domain folding are from Mello & Barrick [72]3}. ΔG° values for consensus TPR folding are from fitted J and H values Kajander et al. [42]5}, as described in the text. ΔG°_intrinsic for the consensus TPR corresponds to folding of a single helix, whereas for the Notch ankyrin domain this value corresponds to folding of an entire repeat. The intrinsic free energy for folding an entire TPR repeat corresponds to twice this value plus a single interfacial term, or +0.16 kcal/mol.