view article
Figure 7
BDamage distribution for different protein sections as identified by STRIDE secondary structure annotation. The seven secondary structure labels are: alpha helix (H), 3–10 helix (G), π-helix (I), extended conformation (E), isolated bridge (b), turn (T) and coil (C, none of the above) (Frishman & Argos, 1995BB10). 33.2% of all residues within the PDB subset were marked alpha helix, 23.4% extended conformation, 19.9% turn, 17.9% coil, 4.3% 3–10 helix, 1.2% isolated bridge, and 0.016% π-helix. Applying Levene's test with median centres (Brown & Forsythe, 1974BB3) for equal variance on a sample of 1500 atoms from each of the seven secondary structure labels, different variances are confirmed (p < 1.1×10-7). All of the distributions are smoothed using a kernel density estimator (R Development Core Team, 2011BB36).

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 22| Part 2| February 2015| Pages 201-212
doi:10.1107/S1600577515002131
Follow J. Synchrotron Rad.
Sign up for e-alerts
E-alerts
Follow J. Synchrotron Rad. on Twitter
Twitter
Follow us on facebook
Facebook
Sign up for RSS feeds
RSS