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. 2015 Jan 27;3:251. Originally published 2014 Oct 24. [Version 3] doi: 10.12688/f1000research.5573.3

Table 6. Properties of the helices of the C-terminal domain of the Zaire Ebola virus nucleoprotein (PDBid:4QAZA).

4QAZA.HELIX0 comprising of residues 646-658 has a reasonably large hydrophobic moment, and has been hypothesized to be part of the protein which is involved in protein-protein interactions 41. Further, these helices have residues with disordered sidechains 41, which are known to be critical for moonlighting functions 39. HM: Hydrophobic moment, RPNR: Ratio of the positive to the negative residues, Len: length of the helix, NCH: number of charged residues.

Helix Len HM RPNR NCH
4QAZA.HELIX0
4QAZA.HELIX1
4QAZA.HELIX2
4QAZA.HELIX3
4QAZA.HELIX4
4QAZA.HELIX5
4QAZA.HELIX6
13
12
3
3
4
3
11
8.4
0.8
2.5
2.4
1.8
0.1
2.1
0.7
0.7
0
0
0.3
-1
1
6
3
1
1
3
0
4