. 2009 Dec 21;19(2):327–348. doi: 10.1002/pro.314

Table VI.

Comparison of Relative Accessible Surface Area in Amyloidogenic and Non-amyloidogenic Helical Residues

			No. of helical residues^a		Average relative ASA per helical residue^b %
Protein	PDB ID	Amyloidogenic sequence(s) containing residues in helical conformation	Amyloidogenic	Nonamyloidogenic	Amyloidogenic	Nonamyloidogenic
α-Synuclein	1XQ8	51–56	28	53	62.5	65.0
		66–74
		77–82
		86–92
β-Lactoglobulin	1BEB dimer	11–20^c	4	28	53.0	39.8
AcP	1APS	16–31^c	7	10	13.8	7.9
Amphoterin	1CKT	12–27	14	34	20.4	34.4
ApoC-II	1SOH	60–70	6	23	56.3	56.1
Insulin	1XDA(1)	13–18	13	14	44.4	41.4
		11–17
Kerato-epithelin	1X3B	515–525 (21–32 in 1X3B)	8	33	33.8	35.1
Lysozyme	1REX	55–61	1	42	0	24.0
Myoglobin	1WLA	101–118	17	94	24.3	31.1
Prolactin	1RW5	7–34	21	97	27.2	25.0
		43–57
hPrP	1QLX	138–144^c	16	38	34.4	37.7
		170–175^c
		178–193^c
repA pPS10	1HKQ dimer	26–34	10	80	12.2	29.2
M. jannaschii tRNA endonuclease	1A79 tetramer	47–53	28	190	2.86	25.9
Enterotoxin, S. aureus	2NTT dimer	50–54	8	58	38.4	16.4
Cytochrome b Rhodobacter sphaeroides	2QJP(1) (Chains A&D)	337–341	10	526	25.0	21.2
Thymidine kinase, cystolic, human	1W4R (Chains A,B,C&D)	133–137	8	167	2.79	24.6
Mean ± SD					28 ± 19	32 ± 14
t-test, t					−0.66
t-test, df					27.49
t-test, P-value					0.52
Mann-Whitney test, P-value					0.49

Secondary structure according to DeepView: Swiss-PdbViewer (Guex and Peitsch, 1997).

Accessible surface area (ASA), average relative surface area per residue (%) computed by the NACCESS program (Hubbard and Thornton, 1993).

One of two or more amyloidogenic sequences in given protein: only this sequence has residues in helical conformation.