论文标题
折叠蛋白的配置熵及其对本质上无序蛋白的重要性
Configurational Entropy of Folded Proteins and its Importance for Intrinsically Disordered Proteins
论文作者
论文摘要
许多成对的添加力场都积极用于本质上无序的蛋白质（IDP）和区域（IDR），其中一些会修改能量术语以改善对IDP/IDR的描述，但在很大程度上与无序状态的解决方案实验分歧。我们已经针对代表性IDP和IDR的实验数据评估了代表性的成对蛋白质和水力场，该肽是经历疾病的过渡疾病的肽，其中七个球状蛋白的大小为130-266氨基酸。我们发现，具有最大统计波动的力场与折叠状态的回旋半径和通用lindemann值一致，同时可以更好地描述IDP和IDRS和IDRS以及为秩序过渡的疾病。因此，要很好地描述IDR/IDP的力场应表现出的症结不仅是蛋白质和水能量之间的平衡，而且是能量效应与球状蛋白质折叠状态的配置熵之间的平衡。
Many pairwise additive force fields are in active use for intrinsically disordered proteins (IDPs) and regions (IDRs), some of which modify energetic terms to improve description of IDPs/IDRs, but are largely in disagreement with solution experiments for the disordered states. We have evaluated representative pairwise and many-body protein and water force fields against experimental data on representative IDPs and IDRs, a peptide that undergoes a disorder-to-order transition, and for seven globular proteins ranging in size from 130-266 amino acids. We find that force fields with the largest statistical fluctuations consistent with the radius of gyration and universal Lindemann values for folded states simultaneously better describe IDPs and IDRs and disorder to order transitions. Hence the crux of what a force field should exhibit to well describe IDRs/IDPs is not just the balance between protein and water energetics, but the balance between energetic effects and configurational entropy of folded states of globular proteins.
