Rapid conformational change results in attractive interactions between biomolecules

疏水相互作用对于生物分子识别是必不可少的。在这个项目中，我们的假设得到了实验数据的证实，即协同的双分子运动导致络合的稳定。对脂肪酸和脂肪酸结合蛋白进行了X-射线分析。结果表明，烷基链长度大于C14的脂肪酸在其末端甲基周围具有高度柔性的构象。这些烷基链的运动很难阻止脂肪酸的高亲和力，从而支持了配体分子的快速运动并不总是降低双分子亲和力，而是稳定了配体的结合。

Hydrophobic interactions are known to be essential for biomolecular recognition. In this project, our hypothesis that concerted bimolecular movements lead to stabilization of complexation was confirmed by experimental data. Fatty acid and fatty-acid binding proteins were subjected to the structural determination by X-ray analysis. The results clearly showed that fatty acids with an alkyl chain longer than C14 have highly flexible conformation around their terminal methyl group. These movements of alkyl chains hardly prevent high affinity of fatty acids, thus supporting that a rapid movements of ligand molecules do not always decrease bimolecular affinity but stabilize the ligand binding.