On 17th September 2018, Raiji Kawade (D2), Departments of Bioengineering, received Student Presentation Award at the 56th Biophysical Society of Japan.
< About awarded research>
Phosphorylation plays critical roles in a wide range of cellular processes such as signaling and on/off switching of interactions.
However, most of the previous studies focusing on the recognition mechanism assumed that the protonation state of a phosphorylated amino acid was PO32- despite the fact that at physiological pH, the phosphate group (pKa ~7) would exist as an equilibrium mixture of PO32– and the singly protonated state (PO3H–).
We performed MD simulations of 4 different proteins-phosphorylated peptide complexes both in the PO32- and PO3H- states. Our study suggested PO32- was more preferable to PO3H- in the interactions due to the larger mobility and higher amount of charge of the phosphate group in the PO32- state.
< Your impression & future plan>
I am very honored to hear that. I very grateful for everyone’s help.
With this study, I will continue my work for the engineering and designing antibodies.