Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy.

Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy.
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DOI:
10.1021/jz101619f
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发表时间:
2011-02-17
期刊:
The journal of physical chemistry letters
影响因子:
--
通讯作者:
Asher SA
Asher SA
中科院分区:
其他
文献类型:
--
作者:
Oladepo SA;Xiong K;Hong Z;Asher SA

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紫外共振拉曼光谱(UVRR)是一种强有力的方法,具有必要的选择性和灵敏度,可以精确地监测溶液中的生物分子结构和动力学。在这个角度来看,我们强调UVRR研究肽和蛋白质的结构和蛋白质和肽的折叠动力学的应用。蛋白质二级结构的UVRR光谱监测器,如酰胺III 3带和Cα-H带的频率和强度,可用于确定肽键的拉氏角分布。这些深刻的,定量的一瞥到构象可以结合动力学T-跳跃方法来监测生物分子构象转变的动力学。由此产生的UVRR结构洞察力令人印象深刻,因为它允许区分,例如,不同的α-螺旋状状态,使π-和310-状态与纯α-螺旋区分开来。这些方法可用于确定沿着最重要的蛋白质折叠坐标沿着的单个肽键的吉布斯自由能。未来的工作将发现光谱监测器,探测控制蛋白质(联合国)折叠机制的肽键激活障碍。此外,侧链振动的UVRR研究将探测侧链在确定蛋白质二级、三级和四级结构中的作用。
UV resonance Raman spectroscopy (UVRR) is a powerful method that has the requisite selectivity and sensitivity to incisively monitor biomolecular structure and dynamics in solution. In this perspective, we highlight applications of UVRR for studying peptide and protein structure and the dynamics of protein and peptide folding. UVRR spectral monitors of protein secondary structure, such as the Amide III3 band and the Cα-H band frequencies and intensities can be used to determine Ramachandran Ψ angle distributions for peptide bonds. These incisive, quantitative glimpses into conformation can be combined with kinetic T-jump methodologies to monitor the dynamics of biomolecular conformational transitions. The resulting UVRR structural insight is impressive in that it allows differentiation of, for example, different α-helix-like states that enable differentiating π- and 310- states from pure α-helices. These approaches can be used to determine the Gibbs free energy landscape of individual peptide bonds along the most important protein (un)folding coordinate. Future work will find spectral monitors that probe peptide bond activation barriers that control protein (un)folding mechanisms. In addition, UVRR studies of sidechain vibrations will probe the role of side chains in determining protein secondary, tertiary and quaternary structures.
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