Table 1.

Secondary structures distribution at protein interface, surface and core

	Interface	Surface	Core	All
Complete dataset
α	25.7	26.8	32.8	28.6
β	18.4	15.9	32.6	21.7
loop	36.3	37.4	23.0	32.6
border	19.6	16.8	13.6	17.1
Homodimers/Heterodimers
α	24.3/19.5	27.1/21.2	32.3/28.5	28.2/22.6
β	18.8/25.2	15.1/20.4	32.1/38.7	21.1/26.0
loop	37.3/36.9	37.6/38.7	23.8/22.3	33.2/34.3
border	19.6/18.4	20.2/19.6	11.1/10.5	23.6/17.1
Obligate/Transient
α	23.5/17.6	26.0/17.4	31.7/24.0	27.5/19.3
β	18.6/22.7	15.0/23.3	29.7/38.9	20.4/27.8
loop	37.5/40.8	38.2/39.9	25.4/26.7	33.8/36.2
border	20.4/18.9	20.8/19.3	13.2/10.4	18.2/16.7
Bound/Unbound
α	15.0/15.0	17.6/17.8	23.7/24.0	19.1/19.4
β	18.2/17.7	21.9/22.0	39.7/40.1	26.9/27.1
loop	46.4/46.8	40.1/40.0	25.1/24.8	36.2/36.2
border	20.2/20.3	20.3/20.0	11.4/11.0	17.6/17.3

Percentage of secondary structures in the three protein compartments Interface, Surface, Core and their global proprotion in proteins (All) are given for the five datasets. Regular secondary structures are evaluated by α- and β-letters, non-regular ones by loop- and border-letters.