. Author manuscript; available in PMC: 2017 Sep 7.

Published in final edited form as: Structure. 2014 Nov 13;22(12):1754–1763. doi: 10.1016/j.str.2014.09.012

Table 1.

NMR-derived kinetic parameters

Protein	Fitted parameters^a		Mean TC^b	Other conditions
	f_i^Ox	TC h
X1NTD	.08	6.33		Standard buffer^c
	.08	7.09
	.08	9.8
	.08	6.72	7.49±0.79
H8Y	0.8	4.31
	.08	6.90
	.08	6.85
	.08	5.81
	.08	5.46	5.87±0.48
S17T	.16	9.92
	.12	10.33
	.12	11.32
	.15	11.68	10.81±0.41
Y30W	.20	8.43
	.16	9.84
	.25	10.12	9.46±0.91
X1NTD	.08	7.80		25 mM HCO_3⁻
	.08	9.20
wt	.08	5.92		20% D₂O
wt	0.17	4.55		10 nM CuCl₂
	0.36	3.03		100 nM CuCl₂
	1.0	-		10 µM CuCl₂
wt	0.18	2.99		2.9 µM PDI
	0.15	1.88		5.8 µM PDI
	0.06	0.70		29 µM PDI

Data for the wt human X1NTD and for each of the four mutants were fit setting f_i^Ox = 0.08, as discussed in methods. Time constants are given in hours. PDI concentration calculated using MW = 57 kD.

Includes standard error calculation.

Unless otherwise indicated studies were done in 25 mM Tris-d11, pH 7.6 (uncorrected), 140mM NaCl, 75mM NaHCO₃, 0.5 mM EDTA, 0.25 mM sodium azide in D₂O.