Table 1.

List of proteins and polypeptides a

No.	Protein	Reference	PDB	L	ln(kf)	CO, %	Abs_CO
30	S6	Otzen and Oliveberg 1999	1RIS	101 (97)	5.9	18.9	18.4
31	His-containing phosphocarrier protein	Van Nuland et al. 1998b	1POH	85	2.7	17.6	15.0
32	N-terminal domain from L9	Kuhlman et al. 1998	1DIV	56	6.1	12.7	7.1
33	Villin 14T	Choe et al. 1998	2VIK	126	6.8	12.3	15.4
34	Apomyoglobinl	Cavagnero et al. 1999	1A6N	151	1.1	8.4	12.7
35	Colicin E7 immunity protein	Ferguson et al. 1999	1CEI	87 (85)	5.8	10.8	9.2
36	Cro protein	Laurents et al. 2000	2CRO	71 (65)	3.7	11.2	7.3
37	P16 protein	Tang et al. 1999	2A5E	156	3.5	5.3	8.3
38	Twitching Ig repeat 27	Fowler and Clarke 2001	1TIT	89	3.6	17.8	15.8
39	CD2, 1st domain	Parker et al. 1997	1HNG	98 (95)	1.8	16.9	16.0
40	Fibronectin tenth FN3 module	Cota and Clarke 2000	1FNF	94	5.5	16.5	15.5
41	IFABP from rat	Burns et al. 1998	1IFC	131	3.4	13.5	17.7
42	ILBPm	Dalessio and Ropson 2000	1EAL	127	1.3	12.3 ± 0.5	15.7 ± 0.6
43	CRBP II	Burns et al. 1998	1OPA	133	1.4	14.0	18.7
44	CRABP I	Burns et al. 1998	1CBI	136	−3.2	13.8	18.8
45	tryptophan synthase α-subunitn	Ogasahara and Yutani 1994	1QOP	268 (267)	−2.5	8.3	22.3
46	GroEL apical domain (191–345)	Golbik et al. 1998	1AON	155	0.8	13.7	21.2
47	Barstaro	Schreiber and Fersht 1993	1BRS	89	3.4	11.8	10.5
48	Che Y	Munoz et al. 1994	3CHY	129 (128)	1	8.7	11.2
49	Ribonuclease HIp	Parker and Marqusee 1999	2RN2	155	0.1	12.4	19.3
50	DHFR (dihydrofolate reductase)q	Jennings et al. 1993	1RA9	159	4.6	14.0	22.3
51	tryptophan synthase β2-subunitn	Goldberg et al. 1990	1QOP	396 (390)	−6.9	8.3	32.5
52	N-terminal domain from PGK	Parker et al. 1995	1PHP	175	2.3	11.5	20.2
53	C-terminal domain from PGKr	Parker et al. 1996	1PHP	219	−3.5	8.0	17.4
54	Barnase	Matouschek et al. 1990	1BNI	110 (108)	2.6	11.4	12.3
55	T4 lysozymes	Parker and Marqusee 1999	2LZM	164	4.1	7.1	11.6
56	Ubiquitint	Khorasanizadeh et al. 1996	1UBQ	76	5.9	15.1	11.5
57	Suc 1u	Schymkowitz et al. 2000	1SCE	113 (101)	4.2	11.8	11.9

^h The folding of mutant protein Y34W was studied experimentally; we used the available PDB structure of wild type in our calculation of CO.

ⁱ The folding of mutant protein Y47W was studied experimentally; we used the available PDB structure of this mutant in our calculation of CO.

^j The folding of mutant protein F56W was studied experimentally; we used the available PDB structure of mutant Y31H/Q36R in our calculation of CO.

^k The folding of mutant protein C21S was studied experimentally; we used the available PDB structure of wild type protein in our calculation of CO.

^l We used the available PDB structure of a holoform of myoglobin (but without heme) in our calculation of CO.

^m We used the available PDB structure of mutant protein T118S from pig in our calculation of CO instead of the wild type protein from rat

ⁿ The folding of protein from Escherichia coli was studied experimentally. We used the available PDB structure of the same protein from Salmonella typhimurium in our calculation of CO.

^o The folding of mutant protein C40A/C82A was studied experimentally; we used the available PDB structure of this mutant in our calculation of CO.

^p The folding of mutant protein C13A/C63A/C133A was studied experimentally; we used the available PDB structure of wild type protein in our calculation of CO.

^q The folding of wild type protein was studied. We used the available PDB structure of mutant protein N37D in our calculation of CO. ln(k_f) value refers to the summary rate of two parallel pathways of refolding of DHFR.

^r The folding of mutant protein W290Y was studied experimentally. We used the available PDB structure of wild type in our calculation of CO.

^s The folding of Cys-free mutant was studied experimentally. We used the available PDB structure of wild-type protein in our calculation of CO.

^t The folding of bovine protein F45W mutant was studied experimentally. We used the available PDB structure of WT human protein in our calculation of CO.

^u There is only a strand-exchanged form of suc1 dimer in PDB. We used a concatenation of fragment 2–88 of chain C and fragment 89–102 of chain A as a tentative structure of monomeric protein in our calculation of CO.