STRUCTURAL COMPARISON OF DENATURED AND SUPERCHARGED PROTEINS IN GAS AND SOLUTION PHASES

The work presented looks at protein stability in the gas phase by directly comparing solution and gas phase structures of "non-native" proteins, specifically denatured and supercharged proteins. Crosslinking coupled to mass spectrometry captures solution and gas phase structures for comparison to discern the extent solution phase structures are retained in the gas phase. Using electron capture fragmentation methods, protein fragmentation patterns are analyzed to identify where crosslinkers are located in order to compare different structural patterns. Ion mobility measurements enable direct comparisons of native and supercharged proteins to identify any structural changes occurring during the supercharging process.