Sikorski A, Kolinski A, Skolnick J
Department of Chemistry, University of Warsaw, Poland.
Proteins. 2000 Jan 1;38(1):17-28.
Reduced lattice models of the three de novo designed helical proteins alpha2, alpha2C, and alpha2D were studied. Low temperature stable folds were obtained for all three proteins. In all cases, the lowest energy folds were four-helix bundles. The folding pathway is qualitatively the same for all proteins studied. The energies of various topologies are similar, especially for the alpha2 polypeptide. The simulated crossover from molten globule to native-like behavior is very similar to that seen in experimental studies. Simulations on a reduced protein model reproduce most of the experimental properties of the alpha2, alpha2C, and alpha2D proteins. Stable four-helix bundle structures were obtained, with increasing native-like behavior on-going from alpha2 to alpha2D that mimics experiment.
研究了三种从头设计的螺旋蛋白α2、α2C和α2D的简化晶格模型。这三种蛋白均获得了低温稳定折叠。在所有情况下，能量最低的折叠都是四螺旋束。所研究的所有蛋白的折叠途径在定性上是相同的。各种拓扑结构的能量相似，尤其是对于α2多肽。从熔球态到类天然行为的模拟转变与实验研究中观察到的非常相似。在简化蛋白质模型上的模拟重现了α2、α2C和α2D蛋白的大部分实验性质。获得了稳定的四螺旋束结构，从α2到α2D，类天然行为不断增加，这与实验结果相似。
