标题： 序列在粗粒度蛋白质模型中决定了扭结程度 显示英文标题

标题： Sequence determines degree of knottedness in a coarse-grained protein model

摘要： 在球状均聚物中，纽结很常见，但在球状蛋白质中却很少见。 为了对这一长期存在的难题提供新的见解，我们在疏水-极性（HP）晶格蛋白质模型的框架下，研究了序列在天然条件下对蛋白质中纽结形成的影响。 通过采用大规模的Wang-Landau模拟结合合适的蒙特卡洛试动，我们发现，尽管平均而言纽结仍然很常见，但序列会引入自纠缠程度的大范围变化。 此外，我们能够设计出要么几乎总是纽结，要么几乎从不纽结的序列。 我们的发现证明了这样一个概念：每个单体仅引入一个额外的自由度（在我们的情况下是序列），就能促进向纽结稀少的蛋白质宇宙演化的可能性。 显示英文摘要

摘要： Knots are abundant in globular homopolymers but rare in globular proteins. To shed new light on this long-standing conundrum, we study the influence of sequence on the formation of knots in proteins under native conditions within the framework of the hydrophobic-polar (HP) lattice protein model. By employing large scale Wang-Landau simulations combined with suitable Monte Carlo trial moves we show that, even though knots are still abundant on average, sequence introduces large variability in the degree of self-entanglements. Moreover, we are able to design sequences which are either almost always or almost never knotted. Our findings serve as proof of concept that the introduction of just one additional degree of freedom per monomer (in our case sequence) facilitates evolution towards a protein universe in which knots are rare.