Stegmann Christian M, Seeliger Daniel, Sheldrick George M, de Groot Bert L, Wahl Markus C
Research Group X-ray Crystallography, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Angew Chem Int Ed Engl. 2009;48(28):5207-10. doi: 10.1002/anie.200900481.
Water molecules doing time: Atomic-resolution crystal structures of the PPIase domain of cyclophilin G, alone and in complex with cyclosporin A, and together with MD simulations and calorimetry, reveal how trapped water molecules influence the thermodynamic profile of a protein-ligand interaction.
亲环蛋白G的肽脯氨酰顺反异构酶结构域单独及与环孢素A形成复合物时的原子分辨率晶体结构，结合分子动力学模拟和量热法，揭示了被困水分子如何影响蛋白质-配体相互作用的热力学特征。
