Table 2.
Secondary structure fractions calculated by deconvolution of circular dichroism spectra. Shown are results for the bacterial thioredoxin-ZnT8A amino terminal domain fusion (TRX-ntZnT8A), the ZnT8A carboxy-terminal domain (ctZnT8A), the carboxy-terminal domain of YiiP (ctYiiP), and bacterial thioredoxin (TRX). Deconvolution solutions produced by the CDSSTR method, using a reference dataset of 128 membrane and soluble protein structures (Abdul-Gader et al., 2011). Secondary structure fractions noted are regular α-helix (αR), distorted α-helix (αD), regular β-strand (βR), distorted β-strand (βD), β-turn (T), and unordered (U), as defined by (Sreerama et al., 1999). The normalized root mean square deviation (NRMSD) is shown for each solution.
protein | αR | αD | βR | βD | T | U | NRMSD |
---|---|---|---|---|---|---|---|
TRX-ntZnT8A | 0.23 | 0.16 | 0.11 | 0.07 | 0.12 | 0.32 | 0.016 |
ctZnT8A | 0.12 | 0.11 | 0.18 | 0.10 | 0.12 | 0.36 | 0.039 |
ctYiiP (X-ray)a | 0.33 | 0.26 | 0.19 | 0.23b | – | ||
TRX | 0.13 | 0.10 | 0.23 | 0.07 | 0.10 | 0.36 | 0.029 |
TRX (X-ray)a | 0.39 | 0.30 | 0.15 | 0.16 | – |
Secondary structure assignment using STRIDE (Kabsch and Sander, 1983).
12% unassigned content and 11% disordered.