Search for: All records

Abstract We report the synthesis and characterization of sulfated pillar[5]arene hosts (P5S₂‐P5S₁₀) that differ in the number of sulfate substituents. All fiveP5S_nhosts display high solubility in water (73–131 mM) and do not undergo significant self‐association according to¹H NMR dilution experiments. The x‐ray crystal structures ofP5S₆,P5S₆ ⋅ Me₆HDA,P5S₈ ⋅ Me₆HDA, andP5S₁₀ ⋅ Me₆HDAreveal one intracavity molecule ofMe₆HDAand several external molecules ofMe₆HDAwhich form a network of close methonium ⋅ ⋅ ⋅ sulfate interactions. The thermodynamic parameters of complexation betweenP5S_nand the panel of guests was measured by direct or competitive isothermal titration calorimetry. We find that the binding free energy toward a guest becomes more negative as the number of sulfate substituents increase. Conversely, the binding free energy of a specific sulfated pillar[5]arene toward a homologous series of guests becomes more negative as the number of NMe groups increases. The ability to tune the host ⋅ guest affinity by changing the number of sulfate substituents will be valuable in supramolecular polymers, separation materials, and latching applications. 

To gain insight into crystalline protein dynamics, we performed molecular-dynamics (MD) simulations of a periodic 2 × 2 × 2 supercell of staphylococcal nuclease. We used the resulting MD trajectories to simulate X-ray diffraction and to study collective motions. The agreement of simulated X-ray diffraction with the data is comparable to previous MD simulation studies. We studied collective motions by analyzing statistically the covariance of alpha-carbon position displacements. The covariance decreases exponentially with the distance between atoms, which is consistent with a liquidlike motions (LLM) model, in which the protein behaves like a soft material. To gain finer insight into the collective motions, we examined the covariance behavior within a protein molecule (intraprotein) and between different protein molecules (interprotein). The interprotein atom pairs, which dominate the overall statistics, exhibit LLM behavior; however, the intraprotein pairs exhibit behavior that is consistent with a superposition of LLM and rigid-body motions (RBM). Our results indicate that LLM behavior of global dynamics is present in MD simulations of a protein crystal. They also show that RBM behavior is detectable in the simulations but that it is subsumed by the LLM behavior. Finally, the results provide clues about how correlated motions of atom pairs both within and across proteins might manifest in diffraction data. Overall, our findings increase our understanding of the connection between molecular motions and diffraction data and therefore advance efforts to extract information about functionally important motions from crystallography experiments.