Table 4.

Correlations between Amino acid Composition of Disordered Proteins and Different Classes of Secondary Structure in Ordered Proteins.

	Exposed Residues				Buried Residues
	Helix	Sheet	Turn	Coil	Helix	Sheet	Turn	Coil	D85
Exposed
Helix	1	0.53	0.44	0.61	0.12	−0.23	−0.04	−0.18	0.64
Sheet	2.6	1	0.38	0.71	−0.04	−0.08	0.01	0.10	0.49
Turn	2.1	1.8	1	0.81	−0.10	−0.28	0.67	0.35	0.74
Coil	3.3	4.3*	5.7*	1	−0.11	−0.33	0.30	0.22	0.85
Buried
Helix	0.5	−0.2	−0.4	−0.5	1	0.80	0.33	0.62	0.08
Sheet	−1.0	−0.4	−1.2	−1.5	5.7*	1	0.28	0.70	−0.20
Turn	−0.2	0.0	3.8	1.3	1.5	1.2	1	0.76	0.32
Coil	−0.8	0.4	1.6	1.0	3.4	4.1*	4.9*	1	0.22
D85	3.5	2.4	4.6*	6.9*	0.3	−0.9	1.4	0.9	1

NOTE.—The t scores for each correlation are shown, and asterisks indicate significance at P <0.05 using the Holm–Bonferroni correction. D, disorder. Information for disordered proteins is based upon the >85% similarity matrix and for ordered proteins is from Goldman, et al. 1998.