Hydrophobic Protein-Ligand Interactions Preserved in the Gas Phase

摘要

The study of the structure and stability of gas-phase noncovalent protein-ligand complexes represents a promising strategy to probe the intrinsic properties of these complexes. Ultimately, new insights about the role of solvent in ligand recognition may be gained from a comparison of protein complexes in the absence and presence of solvent. To date, gas phase studies have focused primarily on protein-ligand complexes stabilized by ionic interactions or hydrogen (H) bonds in solution.These studies have yielded compelling evidence that aspects of solution structure are preserved upon the transfer of protein complexes from solution to the gas phase.