. Author manuscript; available in PMC: 2007 Apr 11.

Published in final edited form as: J Mol Biol. 2006 Oct 6;365(4):1187–1200. doi: 10.1016/j.jmb.2006.09.092

Table 1.

Parameters for urea-induced unfolding for variants of the Notch ankyrin domain containing consensus ankyrin repeats inserted internally

	CD^a						Fluorescence^b
	ΔG^º_{NI, H₂O}	m_NI-value	C_m,NI	ΔG^º_{ID H₂O}	m_IU-value	C_m,IU	ΔG^º_{u H₂O}	m-value	C_m

Nank1-7*	n.a.	n.a.	n.a.	n.a.	n.a.	n.a.	7.64 ± 0.08	2.86 ± 0.02	2.67 ± 0.01
Nank1-5C₁67	2.66 ± 0.24	1.50 ± 0.06	1.77 ± 0.18	7.13 ± 0.17	1.96 ± 0.05	3.61 ± 0.01	8.39 ± 0.09	2.33 ± 0.03	3.60 ± 0.01
Nank1-5C₂67	1.38 ± 0.12	0.83 ± 0.02	1.66 ± 0.15	12.07 ± 0.11	2.10 ± 0.02	5.74 ± 0.01	13.57 ± 0.78	2.36 ± 0.13	5.75 ±0.02

Unfolding free energies, m-values, and unfolding midpoints (C_m) are reported in kcal·mol⁻¹, kcal·mol⁻¹·M⁻¹, and M, respectively. Uncertainties are standard errors on the mean of at least three independent measurements. Conditions: 25 mM Tris·HCl, 150 mM NaCl, pH 8.0, 20ºC.

CD data for Nank1-5C₁,67 and Nank1-5C₂67 were fitted using a three-state model.

Fluorescence data were fitted using a two-state model.