期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 121, 期 13, 页码 2759-2766出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.7b00783
关键词
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资金
- American Society for Mass Spectrometry
- Eli Lilly and Company
- National Institute of General Medical Sciences of the National Institutes of Health [T32GM008268]
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 (Omega) 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 Omega 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 Omega distributions are formed at high energy for disulfide-intact ions from denaturing and from aqueous conditions. The Omega 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 suggegt that specific CAPTR products may be especially sensitive to specific elements of structure in solution.
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