Molecular study of the heterogeneous dynamics behind structure and function in proteins

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K17813
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Physical chemistry
• Research Institution: Institute for Molecular Science
• Principal Investigator: MORI Toshifumi 分子科学研究所, 理論・計算分子科学研究領域, 助教 (20732043)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: 構造変化ダイナミクス / 自由エネルギー / 分子シミュレーション / タンパク質 / 酵素反応 / フォールディング / 時計タンパク質KaiC

Outline of Final Research Achievements

Conformational fluctuations and structural transitions of proteins have become a key to understand the structure and function of proteins. Yet, the molecular origin of these heterogeneous dynamics remains largely elusive. In this project, we have conducted theoretical studies to reveal how protein dynamics play a role in protein folding and function regulation.
First, we developed a theoretical framework to extract slow modes from molecular dynamics trajectories and studied the conformational changes of proteins during folding and function regulation. In particular, we revealed how different folding/unfolding transition pathways and misfolded states lead to heterogeneous dynamics in protein folding.
Secondly, we studied the circadian oscillation in clock protein KaiC of cyanobacteria. As a collaboration with experimental groups, we revealed the molecular mechanism behind the slow ATP hydrolysis, which plays a key role in regulating the circadian oscillation period.

Free Research Field

物理化学、理論化学、生物物理