Ristvejová Jaroslava, Kopecký Vladimír, Sovová Zofie, Balsera Mónica, Arellano Juan B, Green Michael, Ettrich Rüdiger
Laboratory of High Performance Computing, Institute of Systems Biology and Ecology of AS CR, Institute of Physical Biology of USB, Zámek 136, 37333 Nové Hrady, Czech Republic.
Biochem Biophys Res Commun. 2006 Jun 23;345(1):287-91. doi: 10.1016/j.bbrc.2006.04.087. Epub 2006 Apr 27.
Infrared and Raman spectroscopy were applied to identify restraints for the structure determination of the 20 amino acid loop between two beta-sheets of the N-terminal region of the PsbQ protein of the oxygen evolving complex of photosystem II from Spinacia oleracea by restraint-based homology modeling. One of the initial models has shown a stable fold of the loop in a 20 ns molecular dynamics simulation that is in accordance with spectroscopic data. Cleavage of the first 12 amino acids leads to a permanent drift in the root means square deviation of the protein backbone and induces major structural changes.
应用红外光谱和拉曼光谱，通过基于约束的同源建模来确定菠菜光系统II放氧复合体的PsbQ蛋白N端区域两个β折叠之间20个氨基酸环结构的约束条件。在20纳秒的分子动力学模拟中，最初的模型之一显示该环具有稳定的折叠结构，这与光谱数据一致。切除前12个氨基酸会导致蛋白质主链的均方根偏差出现永久性漂移，并引发主要的结构变化。
