writer：Ling SJ, Qi ZM, Knight DP, Huang YF, Huang L, Zhou H, Shao ZZ, Chen X*
keywords：MOLECULAR-CONFORMATION, SECONDARY STRUCTURE
source：期刊
Issue time：2013年

Synchrotron FTIR (S-FTIR) microspectroscopy was used to monitor both protein secondary structures (conformations) and their orientations in single cocoon silk fibers of the Chinese Tussah silk moth (Antheraea pernyi). In addition, to understand further the relationship between structure and properties of single silk fibers, we studied the changes of orientation and content of different secondary structures in single A. pernyi silk fibers when subjected to different strains. The results showed that the content and orientation of beta-sheet was almost unchanged for strains from 0 to 0.3. However, the orientation of alpha-helix and random coil improved progressively with increasing strain, with a parallel decrease in alpha-helix content and an increase in random coil. This clearly indicates that most of the deformation upon stretching of the single fiber is due to the change of orientation in the amorphous regions coupled with a conversion of some of the alpha-helix to random coil. These observations provide an explanation for the supercontraction behavior of certain animal silks and are likely to facilitate understanding and optimization of postdrawing used in the conjunction with the wet-spinning of silk fibers from regenerated silk solutions. Thus, our work demonstrates the power of S-FTIR microspectroscopy for studying biopolymers.