Abstract
The secondary structures of γ44 gliadin and peptides derived from it by enzymic hydrolysis were studied by circular dichroism spectroscopy. Two peptides, obtained by chymotryptic cleavage, broadly corresponding to the proline-rich repetitive N-terminal domain and to the proline-poor non-repetitive C-terminal domain respectively, were studied in detail. A cryogenic solvent system, ethanediol : water (2:1 v/v), was used to determine the cd spectra of the protein and peptides at temperatures down to − 100°C. The proline-rich repetitive peptide showed a spectrum typical of βI/III reverse turns at high-temperature, but a spectrum similar to that of the poly-L-proline II helix at −100 °C. The proline-poor non-repetitive peptide, however, showed an α-helical-type cd spectrum over the temperature range studied. The results are discussed in relation to the conformations of γ-gliadins.
Original language | English |
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Pages (from-to) | 1-13 |
Number of pages | 13 |
Journal | Journal of Cereal Science |
Volume | 11 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1990 |
Externally published | Yes |
Keywords
- 2D-PAGE
- DNA
- HPLC
- SDS-PAGE
- TFA
- cd
- circular dichroism
- deoxyribonucleic acid
- high pressure liquid chromatography
- sodium dodecyl sulphate-polyacrylamide gel electrophoresis
- trifluoroacetic acid
- two dimensional-polyacrylamide gel electrophoresis