Department of Chemistry, Merkert Chemistry Center, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA.
Chemistry. 2012 May 7;18(19):5832-6. doi: 10.1002/chem.201200334. Epub 2012 Mar 30.
CH-π stacks up! Using the protein α(2) D as a model system, we estimate that a CH-π contact between cyclohexylalanine (Cha) and phenylalanine (F) contributes approximately -0.7 kcal mol(-1) to the protein stability. The stacking F-Cha pairs are sequestered in the core of the protein, where water interference does not exist (see figure). Therefore, the observed energetic gain should represent the inherent magnitude and upper limit of the CH-π interactions.
CH-π堆积！我们以蛋白质 α(2)D 作为模型系统进行研究，估计环己基丙氨酸（Cha）和苯丙氨酸（F）之间的 CH-π 接触为蛋白质稳定性贡献约-0.7 kcal mol(-1)。这些堆积的 F-Cha 对被隔离在蛋白质的核心部位，在那里不存在水分子的干扰（见图）。因此，观察到的能量增益应该代表 CH-π 相互作用的固有幅度和上限。
