Effects of Solution Structure on the Folding of Lysozyme Ions in the Gas Phase.

ABSTRACT: The fidelity between the structures of proteins in solution and protein ions in the gas phase is critical to experiments that use gas-phase measurements to infer structures in solution. Here we generate ions of lysozyme, a 129-residue protein whose native tertiary structure contains four internal disulfide bonds, from three solutions that preserve varying extents of the original native structure. We then use cation-to-anion proton-transfer reactions (CAPTR) to reduce the charge states of those ions in the gas phase and ion mobility to probe their structures. The collision cross section (Ω) distributions of each CAPTR product depends to varying extents on the original solution, the charge state of the product, and the charge state of the precursor. For example, the Ω distributions of the 6+

SUBMITTER: Laszlo KJ 

PROVIDER: S-EPMC5486214 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature