Table 1 Relative content of the secondary structure of insulin lysargine in different wavebands.
From: X-ray crystallography reveals insulin lisargine structure and mechanisms of glucose regulation
180–260 | 185–260 | 190–260 | 195–260 | 200–260 | 205–260 | 210–260 | |
|---|---|---|---|---|---|---|---|
α-Helix | n.d | n.d | 45.3% | 45.6% | 42.0% | 36.0% | 40.1% |
Antiparallel | n.d | n.d | 1.2% | 7.3% | 7.9% | 8.5% | 9.5% |
Parallel | n.d | n.d | 8.5% | 7.0% | 5.6% | 5.3% | 5.6% |
β-turn | n.d | n.d | 15.1% | 15.1% | 15.4% | 21.0% | 16.9% |
Rndm. Coil | n.d | n.d | 24.6% | 22.6% | 27.0% | 29.2% | 29.8% |
Total Sum | - | - | 94.7% | 97.7% | 97.8% | 100.0% | 101.9% |
