论文标题
通过粗粒的蒙特卡洛模拟对蛋白质（cove）的热变性
Thermal denaturation of a protein (CoVE) by a coarse-grained Monte Carlo simulation
论文作者
论文摘要
通过粗粒蒙特卡洛模拟研究了蛋白质（Cove）构象的热反应。从其特定的接触曲线验证了三个不同的段，即N末端，跨膜和C末端。发现回旋的半径（RG）表现出非单调的亚近方热响应：在天然相（低温状态）加热时的RG衰变，与在其在变性相中饱和到随机线圈之前的持续升高之前的温度持续升高。蛋白质的球状指数（有效维度的量度）随着蛋白质的腐蚀从球状到随机型构象而降低。
Thermal response of a protein (CoVE) conformation is studied by a coarse-grained Monte Carlo simulation. Three distinct segments, the N-terminal, Trans-membrane, and C-terminal are verified from its specific contact profile. The radius of gyration (Rg) is found to exhibit a non-monotonic sub-universal thermal response: Rg decays on heating in native phase (low-temperature regime) in contrast to a continuous increase on further raising the temperature before its saturation to a random-coil in denature phase. The globularity index (a measure of effective dimension) of the protein decreases as the protein denatures from a globular to a random-coil conformation.
