Division of Theoretical Chemistry , Lund University , 221 00 Lund , Sweden.
Structural Biology and NMR Laboratory, Department of Biology , University of Copenhagen , DK-2200 Copenhagen , Denmark.
J Chem Theory Comput. 2019 Apr 9;15(4):2672-2683. doi: 10.1021/acs.jctc.8b01281. Epub 2019 Mar 27.
The temperature dependence of the conformational properties in simulations of the intrinsically disordered model protein histatin 5 has been investigated using different combinations of force fields, water models, and atomistic and coarse-grained methods. The results have been compared to experimental data obtained from NMR, SAXS, and CD experiments to assess the accuracy and validity of the simulations. The results showed that neither simulations completely agreed with the experimental data, nor did they agree with each other. It was however possible to conclude that the observed conformational changes upon variations in temperature were not at all driven by electrostatic interactions. The final conclusion was that none of the simulations that were investigated in this study was able to accurately capture the temperature induced conformational changes of our model IDP.
已经使用不同的力场、水模型、原子和粗粒方法组合，研究了无规卷曲模型蛋白组蛋白 5 在模拟中的构象特性对温度的依赖性。将结果与从 NMR、SAXS 和 CD 实验获得的实验数据进行了比较，以评估模拟的准确性和有效性。结果表明，没有一个模拟结果完全与实验数据一致，也没有一个模拟结果彼此一致。然而，可以得出结论，在温度变化时观察到的构象变化并非完全由静电相互作用驱动。最终的结论是，在这项研究中，没有一个模拟能够准确捕捉到我们模型 IDP 的温度诱导构象变化。
