Koshi J M, Goldstein R A
Biophysics Research Division, University of Michigan, Ann Arbor, MI 48109-1055, USA.
Pac Symp Biocomput. 2001:191-202. doi: 10.1142/9789814447362_0020.
New computational models of the kinetics of natural site substitutions in proteins are described based on the underlying physical chemical properties of the amino acids. The corresponding reduction in the number of adjustable parameters allows us to analyze site-heterogeneity. Applying this evolutionary model to various data sets allows us to identify the important factors constraining molecular evolution, providing insight into the relationship between amino acid properties and protein structure.
基于氨基酸潜在的物理化学性质，描述了蛋白质中天然位点取代动力学的新计算模型。可调整参数数量的相应减少使我们能够分析位点异质性。将这种进化模型应用于各种数据集，使我们能够识别限制分子进化的重要因素，从而深入了解氨基酸性质与蛋白质结构之间的关系。
