Exploring the “dark matter” of a mammalian proteome by protein structure and function modeling

Table 1 Secondary structure content in sprotein models

Class ^a	Modeled sprotein structures			Best CATH matches
Class ^a	High-quality	Moderate-quality	Low-quality	High-quality	Moderate-quality
α-Helix	0.40 ±0.23	0.34 ±0.24	0.34 ±0.23	0.42 ±0.23	0.42 ±0.25
3-10 Helix	0.02 ±0.03	0.02 ±0.03	0.02 ±0.03	0.03 ±0.03	0.04 ±0.03
π-Helix	0.00 ±0.00	0.00 ±0.00	0.00 ±0.00	0.00 ±0.00	0.00 ±0.00
Extended	0.15 ±0.17	0.10 ±0.12	0.05 ±0.09	0.19 ±0.18	0.17 ±0.16
Isolated bridge	0.01 ±0.01	0.01 ±0.01	0.01 ±0.01	0.01 ±0.01	0.01 ±0.01
Turn	0.22 ±0.09	0.29 ±0.13	0.33 ±0.15	0.19 ±0.08	0.19 ±0.09
Coil	0.20 ±0.08	0.25 ±0.11	0.26 ±0.12	0.16 ±0.05	0.17 ±0.07

^a According to STRIDE classification.
Secondary structure composition of modeled sprotein structures is calculated by STRIDE as a fraction of residues assigned to different secondary structure classes. Sprotein models are compared to a set of the best structural matches identified in the CATH library by Fr-TM-align.

ISSN: 1477-5956