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. Author manuscript; available in PMC: 2010 Mar 4.
Published in final edited form as: J Am Chem Soc. 2009 Mar 4;131(8):2942–2947. doi: 10.1021/ja808305u

Table 1.

Analysis of denaturant-induced CG transition from smFRET experiments

Number Protein n2 Labeling positions 3 Denaturant D504[M] DCG5[M] SN6[Å] SU,0M7[Å] SU,D8[Å] Ref.
1a–1b Barstar 90 12, 89 GdmCl
Urea		 1.24
2.33		 6.4
11.7		 13.3 18.2
24.5		 31.6
30.3		 32
2a CspTm 66 1, 66 GdmCl 2.0 5.3 12.7 20.4 30.2 29
2b–2f CspTm 67 2, 67
10, 67
21, 67
22, 67
34, 67		 GdmCl 2.0
1.7
2.3
1.9
2.4		 3.4
5.1
3.8
4.4
3.4		 12.7 22.5
18.2
20.8
19.8
23.0		 32.4
30.7
32.1
31.5
32.3		 30
3 Im9 86 23, 81 Urea 3.83 8.3 15.5 22.8 36.9 27
4a Protein L 64 1, 64 GdmCl 1.64 6.8 13 17.1 28.9 26
4b Protein L 65 1, 65 GdmCl 2.6 5.8 13 19.8 30.3 29
5 RNaseH 155 3, 135 GdmCl 1.37 3.7 17.1 24.8 50.4 25

Protein abbreviations: Barstar - Ribonuclease inhibitor protein from Bacillus Amyloliquefaciens (PDB: 1BTA), CspTm – Cold-shock protein from Thermotoga Maritima (1G6P), Im9 - immunity protein for colicin E9 (1IMP), Protein L – IgG binding domain B1 of protein L from Peptostreptococcus magnus (1HZ6), RNaseH - Ribonuclease Hi From Escherichia Coli (1RCH).

2

Number of residues.

3

As reported in original references.

4

Denaturation midpoint, as reported in original references, or obtained from a fit of reported denaturation data to a two-state model.

5

CG transition midpoint, defined as the point at which α=1+19/22·φ0 (see Supporting Text).

6

Radius of gyration of native state, calculated using HydroPro from published structures obtained from the Protein Data Bank.

7

Radius of gyration of unfolded state at 0 M denaturant, calculated by extrapolation.

8

Radius of gyration of unfolded state at 6 M GdmCl (8M urea), calculated by extrapolation.