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 |
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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 |