论文标题
热诱导的核蛋白蛋白的核素蛋白的展开重折叠
Thermal induced unfolding refolding of a nucleocapsid COVN protein
论文作者
论文摘要
从其天然构型中的粗粒粒子蛋白的展开显示线性响应，温度升高，然后在其回旋半径中的非单调双峰。该蛋白质符合天然状态的折叠段的随机线圈，在特定温度方案中，脆弱和球状结构的增加，相应结构D的有效尺寸为D约为1.6至2.4。仅热搅拌就不足以完全消除其节段折叠，因为发现很少的折叠在65W，110y，110y，224l，374p之类的残基上，即使在高温下也是如此。
Unfolding of a coarse grained COVN protein from its native configuration shows a linear response with increasing temperature followed by a nonmonotonic double peaks in its radius of gyration. The protein conforms to a random coil of folded segments in native state with increasing tenuous and globular structures in specific temperature regimes where the effective dimensions of corresponding structures D is about 1.6 to 2.4. Thermal agitation alone is not sufficient to fully eradicate its segmental folding as few folds are found to persist around such residues as 65W, 110Y, 224L, 374P even at high temperatures.
