胰凝乳蛋白酶抑制剂的玻璃态以及太赫兹时间尺度下可能与蛋白质功能相关的蛋白质-溶剂波动。
The glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function.
作者信息
Woods Kristina N
机构信息
Physics Department, Carnegie Mellon University, Pittsburgh 15213, PA, USA.
出版信息
BMC Biophys. 2014 Aug 16;7:8. doi: 10.1186/s13628-014-0008-0. eCollection 2014.
BACKGROUND
THz experiments have been used to characterize the picosecond time scale fluctuations taking place in the model, globular protein crambin.
RESULTS
Using both hydration and temperature as an experimental parameter, we have identified collective fluctuations (<= 200 cm(-1)) in the protein. Observation of the protein dynamics in the THz spectrum from both below and above the glass transition temperature (Tg) has provided unique insight into the microscopic interactions and modes that permit the solvent to effectively couple to the protein thermal fluctuations.
CONCLUSIONS
Our findings suggest that the solvent dynamics on the picosecond time scale not only contribute to protein flexibility but may also delineate the types of fluctuations that are able to form within the protein structure.
背景
太赫兹实验已被用于表征球状模型蛋白胰凝乳蛋白酶原发生的皮秒时间尺度波动。
结果
以水合作用和温度作为实验参数，我们识别出了该蛋白中的集体波动（<= 200 cm(-1)）。在玻璃化转变温度（Tg）上下的太赫兹光谱中对蛋白质动力学进行观察，为微观相互作用和模式提供了独特的见解，这些相互作用和模式使溶剂能够有效地与蛋白质热波动耦合。
结论
我们的研究结果表明，皮秒时间尺度上的溶剂动力学不仅有助于蛋白质的灵活性，还可能描绘出能够在蛋白质结构内形成的波动类型。
Zotero 插件