TY - JOUR
T1 - Investigation of the mechanism of photochemically-induced lysozyme crystallization
AU - Okutsu, Tetsuo
AU - Taguchi, Tohru
AU - Korenaga, Jyunya
AU - Kuroiwa, Takashi
AU - Ishikawa, Yu
AU - Iizuka, Shiori
AU - Sugiyama, Kaori
AU - Horiuchi, Hiroaki
AU - Hiratsuka, Hiroshi
N1 - Funding Information:
This study was conducted as a part of the PRESTO project “Innovative use of light and materials/life” funded by the Strategic Basic Research Programs of the National Institute of the Japan Science and Technology Agency .
Publisher Copyright:
© 2016 Elsevier B.V. All rights reserved.
Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 2016/5/1
Y1 - 2016/5/1
N2 - 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.
AB - 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.
KW - Lysozyme
KW - Photo-induced crystallization
KW - Template
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U2 - 10.1016/j.jphotochem.2016.01.026
DO - 10.1016/j.jphotochem.2016.01.026
M3 - Article
AN - SCOPUS:84958025745
SN - 1010-6030
VL - 321
SP - 180
EP - 186
JO - Journal of Photochemistry and Photobiology A: Chemistry
JF - Journal of Photochemistry and Photobiology A: Chemistry
ER -