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Table 1 Secondary structures distribution at protein interface, surface and core

From: Deciphering the shape and deformation of secondary structures through local conformation analysis

 

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

  1. 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.