Yaşar Fatih, Jiang Ping, Hansmann Ulrich H E
Department of Physics Engineering, Hacettepe University, Ankara, 06800, TURKEY.
Department of Chemistry & Biochemistry, University of Oklahoma, Norman, OK 73019-5251, USA.
Europhys Lett. 2014 Feb 1;105(3):30008. doi: 10.1209/0295-5075/105/30008.
We describe multicanonical molecular dynamic simulations of the N-terminal domain of the protein L9. Analyzing free energy landscapes and thermal ordering, we propose a possible folding mechanism for the protein. By comparing our results with that of molecular dynamics runs of the protein at constant temperature, we find that multicanonical molecular dynamics leads to orders of magnitude higher sampling of folding transitions.
我们描述了蛋白质L9 N端结构域的多规范分子动力学模拟。通过分析自由能景观和热有序性,我们提出了该蛋白质可能的折叠机制。通过将我们的结果与该蛋白质在恒温下的分子动力学模拟结果进行比较,我们发现多规范分子动力学导致折叠转变的采样数量提高了几个数量级。