Siebert K J
Department of Food Science and Technology, Cornell University, Geneva, New York 14456, USA.
J Agric Food Chem. 2001 Feb;49(2):851-8. doi: 10.1021/jf000718y.
A quantitative structure-activity relationship (QSAR) modeling approach based on the location of each amino acid along three axes obtained by principal component analysis (called z scores) was extended to physical and functional properties of proteins, where the proportion of particular amino acids rather than a precise sequence is the determining factor. Coomassie Brilliant Blue spectral responses to amino acid homopolymers (R = 0.926) and proteins, either as a function of their contents of six basic and aromatic amino acids (R = 0.976) or as a function of the contributions of these amino acids to the three z scores (R = 0.935), were modeled. The ultraviolet absorbance of proteins was modeled in terms of the z score contributions of tyrosine, tryptophan, and cysteine (R = 0.995). Modeling many protein functional properties in this manner appears to be possible. An approach to modeling peptide behaviors that depend on short sequences of amino acids was also considered.
一种基于主成分分析得到的沿三个轴(称为z分数)的每个氨基酸位置的定量构效关系(QSAR)建模方法被扩展到蛋白质的物理和功能特性,其中特定氨基酸的比例而非精确序列是决定因素。考马斯亮蓝对氨基酸均聚物的光谱响应(R = 0.926)以及对蛋白质的光谱响应,分别作为其六种碱性和芳香族氨基酸含量的函数(R = 0.976)或作为这些氨基酸对三个z分数贡献的函数(R = 0.935)进行建模。蛋白质的紫外吸光度根据酪氨酸、色氨酸和半胱氨酸的z分数贡献进行建模(R = 0.995)。以这种方式对许多蛋白质功能特性进行建模似乎是可行的。还考虑了一种对依赖于氨基酸短序列的肽行为进行建模的方法。