Table 2.

Secondary structure preferences of hydrophobic amino acids indicated by numbers of observations.

		DS1 Dataset		DS2 Dataset
	Secondary	Count in	Count in	Count in	Count in
Residue	Structure	Standard min. g.	Wide min. g.	Standard min. g.	Wide min. g.
ALA	$\alpha$-helix	8	26	8	14
	$\beta$-strand	0	10	0	9
	others	13	5	12	5
	unassigned	12	9	12	8
GLY	bend	28	6	27	6
	turn	22	7	22	7
	$\beta$-strand	0	19	0	10
	others	13	7	13	4
	unassigned	19	6	19	5
ILE	$\beta$-strand	2	18	2	15
	$\alpha$-helix	4	3	4	1
	others	2	2	2	3
	unassigned	5	1	5	0
LEU	$\alpha$-helix	4	14	4	6
	$\beta$-strand	1	8	1	2
	others	4	3	4	1
	unassigned	2	1	2	0
PHE	3-10-helix	8	2	8	2
	$\alpha$-helix	2	15	2	6
	others	5	6	4	2
	unassigned	4	12	4	4
TYR	$\alpha$-helix	4	7	4	4
	others	9	2	9	2
	unassigned	10	1	10	1
VAL	$\beta$-strand	1	17	1	5
	$\alpha$-helix	3	7	3	5
	others	3	2	3	2
	unassigned	7	2	7	1