This work examined the mechanism involved in photoinduced crystallization of a lysozyme, focusing on the structure of the photoproducts that lead to crystal growth. It was determined that dimers formed via linking of tryptophan (Trp) residues are preferentially produced when applying a high-excitation photon fluence. However, these dimers do not lead to crystal growth. A low fluence forms dimers via the combination of tyrosine (Tyr) residues, generating six types of Tyr-Tyr dimers. The dimer that originates from the linking of Tyr53 and Tyr53 has a configuration similar to that of the two adjacent, yet non-linked, lysozyme molecules in the crystal unit cell. The Tyr53-Tyr53 dimer hence acts as a template for lysozyme crystal nucleation.
|ジャーナル||Journal of Photochemistry and Photobiology A: Chemistry|
|出版ステータス||Published - 2016 5 1|
ASJC Scopus subject areas
- 化学 (全般)