[The secondary structure of winter-wheat-bran antifreeze protein determined by FTIR and CD spectrum].

The secondary structure of winter wheat bran antifreeze protein was analyzed by FTIR and CD spectra. The characteristic peaks of the secondary structure of the winter wheat bran antifreeze protein were overlapped from the FTIR analysis. The overlapped peaks of amide I and III of the winter wheat bran antifreeze protein were fitted by the Gauss peak to show the characteristic peaks of the alpha-helix, beta-sheet, beta-turn and random coil. The CD spectrum was evaluated by the Chen-Yang principle and analyzed by the least squares method. Furthermore, the difference between the two analyses was discussed. The final results showed that the alpha-helix, beta-sheet, beta-turn and random coil of the winter wheat bran antifreeze protein was 15.05%-15.87%, 36.00%-36.92%, 17.31%-17.75%, and 30.303-30.82%, respectively. The result would be helpful to the study of the antifreeze mechanism of the winter wheat bran antifreeze protein.