Table 2 Estimation of the secondary structure content of the prepared proteins using the least-squares method (LSA)51 analysing amide I & II bands in infrared spectra (N marks values normalized to 100%).

From: Production of recombinant soluble dimeric C-type lectin-like receptors of rat natural killer cells

NKR-P1BWAG

Clr-11

mouse Clr-g

Structure

LSA (%)

LSA N (%)

LSA (%)

LSA N (%)

crystal structure*

α-helix

21 ± 10

20

23 ± 10

22

17

β-sheet

28 ± 9

27

25 ± 9

24

27

β-turn

14 ± 4

13

13 ± 4

12

12

Bend

15 ± 4

14

14 ± 4

13

15

Disordered

27 ± 6

26

30 ± 6

29

29

Sum

105%

100%

105%

100%

100%

NKR-P1BSD monomer

NKR-P1BSD dimer

NKR-P1BSD dimer

Structure

LSA (%)

LSA N (%)

LSA (%)

LSA N (%)

crystal structure*

α-helix

23 ± 10

22

23 ± 10

22

19

β-sheet

28 ± 9

26

28 ± 9

26

28

β-turn

14 ± 4

13

14 ± 4

13

15

Bend

16 ± 4

15

16 ± 4

15

13

Disordered

26 ± 6

24

26 ± 6

24

25

Sum

107%

100%

107%

100%

100%

  1. Given standard deviations are calculated as standard deviations of the used reference set; therefore, they do not reflect the quality of the fits. *Calculated using DSSP58 on the crystal structures of mouse Clr-g (PDB ID 3RS1)29 and rat NKR-P1BSD dimer (PDB ID 5J2S). However, in the NKR-P1BSD crystal structure, only 118 amino acid residues are visible, i.e., 29 residues (20%), fewer than those present in the expressed protein construct.Given standard deviations are calculated as standard deviations of the used reference set; therefore, they do not reflect the quality of the fits.
Back to article page