In a project of revealing gyro-optical properties of amino acids that build up proteins, all the components of the gyration tensor and the birefringence of L-aspartic acid have been successfully measured as a function of temperature although the crystal belongs to the monoclinic system. The temperature dependence of the rotation of the gyration surface around the crystallographic b axis was also clarified. It is of interest that the chirality index of this crystal was found to be almost the same as that of glutamic acid, another amino acid.
|Number of pages||9|
|Journal||Acta Crystallographica Section A: Foundations of Crystallography|
|Publication status||Published - 1997|
ASJC Scopus subject areas
- Structural Biology