[5a-A502-1~12] 12.7 Biomedical Engineering and Biochips

[5a-A502-6] Theoretical study on Calmodulin binding with Ca(II) and Eu(III) ions

Satoru Tsushima^1,2, 〇Yuji Mochizuki^3,4, Yuto Komeiji⁵, Kouji Okuwaki³, Takaya Abe³, Hirotoshi Mori⁶, Shigenori Tanaka⁷ (1.HZDR, 2.Tokyo Inst. Tech., 3.Rikkyo Univ., 4.Univ. Tokyo, 5.AIST, 6.Ochanomizu Univ., 7.Kobe Univ.)

Keywords:Calmodulin, Molecular Dynamics Simulations, Fragment Molecular Orbital Calculations

Camodulin (CaM) is a Ca(II)-binding protein consisting of 148 amino acid residues, and the number of binding sites is 4. Other heavy metal ions could bind with CaM, leading a denature. The experimental data have been available for the Eu-CaM (with Eu(III)). In this presentation, we will present the computational investigations based on the calculations both of molecular dynamics (MD) and of fragment molecular orbital (FMO).