Table 1.

Calculated nonpolar solvent-accessible surface area at several potential stages of folding in myoglobin in Ų

Residue	Helix position	Local helix	ABGH subdomain	Δ(Local helix-ABGH)	Native myoglobin
TRP 7	A5	135	94.8	40.5	6.48
LEU 9	A7	121	54.9	66.4	54.9
VAL 10	A8	88.4	14.1	74.2	0.09
LEU 11	A9	103	103	0	41.9
VAL 13	A11	91.9	1.13	90.8	1.13
TRP 14	A12	128	107	20.8	11.0
ALA 15	A13	50.7	50.7	0	50.7
VAL 17	A15	70.7	9.29	61.4	2.25
VAL 21	B2	127	83.9	43.2	33.7
ALA 22	B3	73.5	73.5	0	23.8
ILE 28	B9	112	21.4	90.9	4.09
LEU 29	B10	94.3	83.1	11.3	6.33
ILE 30	B11	89.1	89.1	0	14.0
LEU 32	B13	115	37.2	77.7	12.8
PHE 33	B14	132	132	0	2.64
ILE 101	G2	146	59.6	86.7	40.1
TYR 103	G4	78.8	75.5	3.31	17.6
LEU 104	G5	120	38.7	81.1	17.0
PHE 106	G7	107	89.7	17.8	28.5
ILE 107	G8	111	50.1	60.5	33.6
ALA 110	G11	52.7	2.84	49.8	2.84
ILE 111	G12	90.4	34.2	56.2	9.69
ILE 112	G13	110	18.0	92.3	18.0
VAL 114	G15	74.7	11.1	63.5	11.1
LEU 115	G16	110	2.83	108	2.83
PHE 123	GH5	0	0	0	0
ALA 125	H2	72.7	72.7	0	72.7
ALA 127	H4	59	6.39	52.6	6.39
ALA 130	H7	54.9	1.13	53.7	0.49
MET 131	H8	115	6.54	108	2.07
ALA 134	H11	48.2	12.4	35.8	0.20
LEU 135	H12	84.6	26.5	58.1	2.65
LEU 137	H14	109	85.3	23.5	23.6
PHE 138	H15	129	105	24.5	20.8
ILE 142	H19	74.7	49.1	25.6	0.96
ALA 143	H20	51.6	30.5	21.2	15.7
ALA 144	H21	57.4	57.4	0	57.2
TYR 146	H23	111	78.6	32.5	6.34
LEU 149	H26	103	103	0	40.1

Local helix refers to the isolated helix in which the residue is located. The ABGH subdomain refers to these helices plus the AB and GH loops in the myoglobin structure. Native myoglobin refers to the fully folded protein (as described by the complete crystal structure). Only hydrophobic residues in the A, B, G, and H helices are listed.