総説 |
共鳴効果を利用する生体分子の部位特異的ダイナミクス観測 Site-specific Observation of Dynamics in Biological Molecules utilizing Resonance Effect 水野 操・水谷 泰久 タンパク質は構造を変化させて機能する.そのダイナミクスは,サブピコ秒から秒,サブオングストロームから数十オングストロームと時間・空間の幅広いスケールにわたる.そして,それらは互いに連動することによって機能に必須な動きを生み出している.筆者らは,時間分解共鳴ラマン分光法の特色を活かして,機能に関わるタンパク質ダイナミクスを調べている.本稿では,「連動性」をキーワードとして,この分野の進展を解説する. Protein dynamics are intimately connected to the structure/function relationship of biological systems. The dynamics spans over a wide range of time scales from the earliest moments, such as the picosecond regime, toward time scales highly relevant to biological functions, such as the microsecond or millisecond regimes. We have been studying protein dynamics by using time-resolved resonance Raman spectroscopy, which is sufficiently structure sensitive at a chemical-bond resolution. One of the advantages of resonance Raman spectroscopy over other spectroscopy is selectivity due to resonance effect. By taking advantage of resonance effect, we can investigate specific parts of protein by using different excitation wavelengths. Thus, this technique is suitable for examining how proteins change their shape in response to external stimuli. In this review, we summarize recent progresses in resonance Raman studies on protein dynamics.
Keywords:resonance Raman spectroscopy, time-resolved spectroscopy, protein dynamics
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