Institut Pasteur de Montevideo, Mataojo 2020, Montevideo, CP 11400, Uruguay.
Graduate Program in Chemistry, Facultad de Química, Universidad de la República, Montevideo 11800, Uruguay.
J Chem Theory Comput. 2021 Feb 9;17(2):599-604. doi: 10.1021/acs.jctc.0c00948. Epub 2021 Jan 7.
The challenges posed by intrinsically disordered proteins (IDPs) to atomistic and coarse-grained (CG) simulations are boosting efforts to develop and reparametrize current force fields. An assessment of the dynamical behavior of IDPs' and unstructured peptides with the CG SIRAH force field suggests that the current version achieves a fair description of IDPs' conformational flexibility. Moreover, we found a remarkable capability to capture the effect of point mutations in loosely structured peptides.
具有内在无序结构的蛋白质 (IDPs) 给原子和粗粒 (CG) 模拟带来了挑战，这推动了开发和重新参数化现有力场的努力。使用 CG SIRAH 力场评估 IDPs 和无规多肽的动力学行为表明，当前版本能够很好地描述 IDPs 的构象灵活性。此外，我们发现该力场在捕捉结构松散的多肽中定点突变的效果方面具有显著的能力。
