Abstract
We have used circular dichroism spectroscopy and structure prediction to study the secondary structure of a group of gluten proteins. They have short α-helices at the N- and C-termini, which are cross-linked by disulphide bonds. The long repetitive central domain has regular β-turns. This structure is similar to that previously proposed for elastin, suggesting a common molecular basis for elasticity. Wheat Gluten protein Secondary structure Elasticity.
| Original language | English |
|---|---|
| Pages (from-to) | 205-208 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 177 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 19 Nov 1984 |
| Externally published | Yes |