Effects of Solution Structure on the Folding of Lysozyme Ions in the Gas Phase
| Autor: | Kenneth J. Laszlo, Matthew F. Bush, Eleanor B. Munger |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Protein Folding
Protein Conformation 010402 general chemistry 01 natural sciences Article Ion Gas phase chemistry.chemical_compound Cross section (physics) Egg White Materials Chemistry Animals Physical and Theoretical Chemistry Ions Quantitative Biology::Biomolecules Chemistry 010401 analytical chemistry Charge (physics) Protein tertiary structure 0104 chemical sciences Surfaces Coatings and Films Solutions Folding (chemistry) Crystallography Chemical physics Product (mathematics) Muramidase Gases Lysozyme Chickens |
| Zdroj: | The Journal of Physical Chemistry B. 121:2759-2766 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/acs.jpcb.7b00783 |
| Popis: | 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+ ions depend strongly on the original solutions conditions and to a lesser extent on the charge state of the precursor. Energy-dependent experiments suggest that very different structures are accessible to disulfide-reduced and disulfide-intact ions, but similar Ω distributions are formed at high energy for disulfide-intact ions from denaturing and from aqueous conditions. The Ω distributions of the 3+ ions are all similar but exhibit subtle differences that depend more strongly on the original solutions conditions than other factors. More generally, these results suggest that specific CAPTR products may be especially sensitive to specific elements of structure in solution. |
| Databáze: | OpenAIRE |
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