Glazer A N
Proc Natl Acad Sci U S A. 1970 Apr;65(4):1057-63. doi: 10.1073/pnas.65.4.1057.
Strong binding of dyes to simple globular proteins takes place predominantly in areas overlapping the binding sites for substrates, coenzymes and prosthetic groups, in preference to other regions of the protein surface. The structure of the dyes bears no obvious relationship to that of the normal ligands. It is proposed that this phenomenon is a reflection of the special stereochemical features of such sites, their hydrophobicity relative to other portions of the protein surface, and, possibly, greater flexibility in these regions of the protein molecule. The binding properties of antibodies and bovine serum albumin are discussed in relation to this apparent versatility of protein binding sites towards structurally unrelated organic ligands.
染料与简单球蛋白的强烈结合主要发生在与底物、辅酶和辅基结合位点重叠的区域，而不是蛋白质表面的其他区域。染料的结构与正常配体的结构没有明显关系。有人提出，这种现象反映了这些位点的特殊立体化学特征、它们相对于蛋白质表面其他部分的疏水性，以及蛋白质分子这些区域可能更大的灵活性。结合抗体和牛血清白蛋白的结合特性，讨论了蛋白质结合位点对结构不相关有机配体的这种明显通用性。
