Koshi J M, Goldstein R A
Biophysics Research Division, University of Michigan, Ann Arbor 48109-1055, USA.
Proteins. 1998 Aug 15;32(3):289-95.
New computational models of natural site mutations are developed that account for the different selective pressures acting on different locations in the protein. The number of adjustable parameters is greatly reduced by basing the models on the underlying physical-chemical properties of the amino acids. This allows us to use our method on small data sets built of specific protein types. We demonstrate that with this approach we can represent the evolutionary patterns in HIV envelope proteins far better than with more traditional methods.
我们开发了新的自然位点突变计算模型，该模型考虑了作用于蛋白质不同位置的不同选择压力。通过基于氨基酸的基本物理化学性质构建模型，可大幅减少可调参数的数量。这使我们能够将我们的方法应用于由特定蛋白质类型构建的小数据集。我们证明，通过这种方法，我们能够比使用更传统的方法更好地呈现HIV包膜蛋白中的进化模式。
